| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| Purified | NBP3-25349-0.025mg | |||
| Purified | NBP3-25349-0.05mg | |||
| BSA Free | NB100-142SS | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB100-143SS | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB110-57130SS | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB100-56506SS | |||
| Azide and BSA Free | NBP2-33212 | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB100-104SS | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB100-154SS | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB100-306SS | |||
| Azide and BSA Free | NBP2-80586 | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NBP1-81445-25ul | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB100-56694SS | |||
![Simple Western: Mre11 Antibody [NB100-142] - Image shows a specific band for Mre11 in 0.5 mg/mL of HeLa lysate. A band appears at the theoretical molecular weight of 81 kDa for this product. This experiment was performed under reducing conditions using the 12-230 kDa separation system.](http://images.novusbio.com/fullsize/Mre11-Antibody-Simple-Western-NB100-142-img0010.jpg "Simple Western: Mre11 Antibody [NB100-142] - Image shows a specific band for Mre11 in 0.5 mg/mL of HeLa lysate. A band appears at the theoretical molecular weight of 81 kDa for this product. This experiment was performed under reducing conditions using the 12-230 kDa separation system.")
![Immunocytochemistry/Immunofluorescence: Mre11 Antibody [NB100-142] - IF analysis of Mre11 on HeLa. Image from verified customer review.](http://images.novusbio.com/fullsize/Mre11-Antibody-Immunocytochemistry-Immunofluorescence-NB100-142-img0009.jpg)
![<b>Genetic Strategies Validation. </b>Western Blot: Mre11 Antibody [NB100-142] - Mre11 and NBS1 contribute to OriP replication and EBV episome stability. D98/HR1 cells were transfected with siRNA for Mre11 or NBS1, or Luciferase control and assayed by immunoblot (IB) with antibodies specific for Mre11 (left pane) or NBS1 (right panel), or PCNA (lower panel) as a loading control. Image collected and cropped by CiteAb from the following publication (//journals.plos.org/plosone/article?id=10.1371/journal.pone.0001257) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/Mre11-Antibody-Knockdown-Validated-NB100-142-img0012.jpg)
![Immunohistochemistry: Mre11 Antibody [NB100-142] - Immunohistochemical staining of MRE11 in a human epidermis cross section.](http://images.novusbio.com/fullsize/Mre11-Antibody-Immunohistochemistry-NB100-142-img0004.jpg)
![Western Blot: Mre11 Antibody [NB100-142] - Western blot analysis of Mre11 on 50 ug of HeLa and MEF lysates, displaying bands at the molecular weight of 81 kDa.](http://images.novusbio.com/fullsize/Mre11-Antibody-Western-Blot-NB100-142-img0005.jpg)
![Immunocytochemistry/Immunofluorescence: Mre11 Antibody [NB100-142] - HeLa cells were fixed for 10 minutes using 10% formalin and then permeabilized for 5 minutes using 1X TBS + 0.5% Triton X-100. The cells were incubated with anti-Mre11 [NB100-142] at a 1:500 dilution overnight at 4C and detected with an anti-rabbit DyLight 488 (Green) at a 1:500 dilution. Actin was detected with Phalloidin 568 (Red) at a 1:200 dilution. Nuclei were counterstained with DAPI (Blue). Cells were imaged using a 40X objective.](http://images.novusbio.com/fullsize/Mre11-Antibody-Immunocytochemistry-Immunofluorescence-NB100-142-img0011.jpg)
![Chromatin Immunoprecipitation: Mre11 Antibody [NB100-142] - Aggregated END-seq signal and MRE11 ChIP-seq RPM in WT (left) and Atm -/- (right). To fairly compare ChIP-seq signal between WT and Atm -/-, MRE11 scale is proportional to spike-in normalized END-seq RPM for each genotype. Individual hotspot examples (chr12:34,592,264-34,598,265) are shown below. Note that decreased MRE11 coverage is observed within NDR of Atm -/-. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32051414/) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/Mre11 Antibody-Chromatin Immunoprecipitation-NB100-142-img0013.jpg)
![<b>Genetic Strategies Validation. </b>Western Blot: Mre11 Antibody [NB100-142] - TIG-1 human primary fibroblasts, whole cell lysate (30 ug). Image from verified customer review.](http://images.novusbio.com/fullsize/Mre11-Antibody-Knockdown-Validated-NB100-142-img0008.jpg)
![Western Blot: Mre11 Antibody [NB100-142] - MRE11 associates with the DS region of OriP.A) DNA affinity purification assays were performed with Raji nuclear extracts & DNA templates derived from DS wt, DS nm-, or delta DS. Input & template bound proteins were analyzed by Western blot with antibodies to TRF2, MRE11, EBNA1, PCNA, & PARP1, as indicated. B) Schematic of template DNA used for DNA affinity purification in A, & their respective protein binding sites. C) ChIP assays to monitor EBNA1, TRF2, & MRE11 binding at OriP wt or OriP nm- in transfected 293 cells. Immunoprecipitated DNA was quantified by real time PCR relative to total input DNA recovered for each transfected cell. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/18040525), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-142_rabbit-polyclonal-mre11-antibody-310202415384114.jpg)
![Western Blot: Mre11 Antibody [NB100-142] - Immunoblotting analysis of IR-induced AKT (Ser473) activation. (A) The levels of AKT activation were measured by AKT Ser473 phosphorylation in 293T, 293T/eIF3f & 293T/eIF3f-hMSH4 cells treated with 10 Gy IR in comparison to untreated controls. Levels of p53 Ser15 phosphorylation & the total protein levels of AKT, hMRE11 & p53 were also analyzed. alpha -tubulin was used as a loading control. (B) The levels of Chk2 activation (Chk2 Thr68 phosphorylation) in 293T, 293T/eIF3f & 293T/eIF3f-hMSH4 cells in response to 10 Gy IR. Cell lysates were prepared at 1 hr post IR treatment. Untreated cells were analyzed as controls, while alpha -tubulin was used as a loading control. Image collected & cropped by CiteAb from the following publication (//molecular-cancer.biomedcentral.com/articles/10.1186/1476-4598-12-51), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-142_rabbit-polyclonal-mre11-antibody-310202415293334.jpg)
![Western Blot: Mre11 Antibody [NB100-142] - The DNA damage response at telomeres uncapped through TRF2 depletion does not require BRCA1 or CtIPImmortalized Brca1F/− MEFs were infected with retroviruses expressing the indicated shRNAs and/or Cre recombinase, followed by selection with puromycin for 72 h. Cell extracts were prepared 48 h later & analysed by Western blotting as indicated. SMC1 & tubulin were used as loading controls. *non-specific band.Cells treated as in (A) were fixed 48 h after selection & stained with an anti-53BP1 antibody (green). Telomeres were visualized with a Cy3-conjugated (CCCTAA)3-PNA probe (red). Yellow arrowheads point to 53BP1 foci that co-localize with telomeres.Quantification of TIFs in cells treated as in (B). A minimum of 200 nuclei were scored for each sample. Error bars represent SD of two independent experiments. P-values were calculated using an unpaired two-tailed t-test. *P ≤ 0.05; NS, P > 0.05. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/25582120), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-142_rabbit-polyclonal-mre11-antibody-31020241554548.jpg)
![Western Blot: Mre11 Antibody [NB100-142] - MRE11 & NBS1 contribute to OriP replication & EBV episome stability.A) D98/HR1 cells were transfected with siRNA for MRE11 or NBS1, or Luciferase control & assayed by immuno-blot (IB) with antibodies specific for MRE11 (left pane) or NBS1 (right panel), or PCNA (lower panel) as a loading control. B) Transient DNA replication assays of OriP-containing plasmids were analyzed by Southern blot. D98/HR1 cells were transfected with OriP plasmid & siRNA for either MRE11, NBS1, or luciferase control (as indicated above each lane). Hirt extracted plasmid DNA was digested with DpnI plus BamHI (top panel) or BamHI only (lower panel) & probed with OriP specific probes. DNA was quantified by PhosphorImager analysis & the replication value was determined as the ratio of DpnI/BamHI to BamHI recovered products. Quantification shown below is a summary of at least four independent replication assays (data not shown). C)) EBV episomes from latently infected D98/HR1 cells were analyzed by pulse field electrophoresis & Southern blotting after transfection of siRNA for control (siLuc), MRE11, or NBS1. Raji cells were used as a control for EBV episome size & abundance. The percentage of EBV episomes relative to the EBV DNA retained in the well is calculated below. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/18040525), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-142_rabbit-polyclonal-mre11-antibody-310202416574.jpg)
![Western Blot: Mre11 Antibody [NB100-142] - Evidence that MRE11 & NBS1 are required for EBV episome maintenance.A) OriP plasmid maintenance assays were performed in MRE11 mutant (ATLD3) & reconstituted (ATLD3/wtMRE11) cell lines (left panel) or NBS1 mutant (GM7166) & reconstituted (GM7166/wtNBS1) cell lines (right panel). Plasmids containing OriP & EBNA1 were monitored by Southern blotting of Hirt lysates at 1 (lower panel) & 7 (upper panel) days post-transfection. Phosphorimager quantification of four independent experiments as shown in panal A where maintenance is measured as the ratio of day 7 to day 1 for OriP plasmid detection is shown below. B) EBV transformed B-lymphocytes were analyzed by PFG & Southern blotting for the presence of episomal forms of the EBV genome. Raji, Namalwa, NBS1 (GM15808), NBS1 (GM07078), LCL3472, & LCLAW7 DNA was loaded at equal concentrations & analyzed by ethidium staining of PFG (lower panel) or by Southern blot (upper panel) with EBV specific probe. C) Western blot of the same cell lines used for PFG analysis shown in panel B was probed with antibodies specific for NBS1 (antibody 143 & antibody 277), MRE11, or loading control Actin. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/18040525), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-142_rabbit-polyclonal-mre11-antibody-31020241612675.jpg)
![Western Blot: Mre11 Antibody [NB100-142] - Involvement of CBP & p300 in the transcription of the BRCA1 & RAD51 genes.(A) Down-regulation of BRCA1 & RAD51 proteins upon depletion of CBP and/or p300. H1299 cells were transfected for 48 hr with non-targeting (siNT), CBP (siCBP), p300 (sip300), or CBP+p300 (siC+p) siRNAs. The cells were harvested & whole cell extracts were subjected to immunoblotting. (B, C) Reduction of BRCA1 & RAD51 transcripts in CBP- & p300-depleted cells. H1299 cells were transfected for 48 hr with non-targeting (siNT), CBP (siCBP), p300 (sip300), or CBP+p300 (siC+p) siRNAs. Cells were harvested & subjected to quantitative real-time PCR for the detection of BRCA1 (B) & RAD51 (C) mRNAs. Expression levels were normalized against the levels of GAPDH mRNA. Data represent the mean ± SD. (D) H1299 cells were transfected for 48 hr with non-targeting (siNT), CBP (siCBP), p300 (sip300), or CBP+p300 (siC+p) siRNAs, & stained with propidium iodide (PI). The percentage of cells in each cell cycle phase was determined by FACS. Percentages of cells in G1, S, & G2/M are shown. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/23285190), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-142_rabbit-polyclonal-mre11-antibody-310202415525210.jpg)
![Western Blot: Nbs1 Antibody [NB100-143] - Lysates of HeLa human cervical epithelial carcinoma parental cell line and Nbs1 knockout (KO) HeLa cell line. PVDF membrane was probed with 1:1000 of Rabbit Anti-Human Polyclonal [NB100-143] followed by HRP-conjugated Anti-Rabbit IgG Secondary Antibody (HAF008). Specific band was detected for Nbs1 at approximately 95 kDa (as indicated) in the parental HeLa cell line, but is not detectable in the knockout HeLa cell line. This experiment was conducted under reducing conditions.](http://images.novusbio.com/fullsize/Nbs1-Antibody-Knockout-Validated-NB100-143-img0015.jpg "<b>Genetic Strategies Validation. </b>Western Blot: Nbs1 Antibody [NB100-143] - Lysates of HeLa human cervical epithelial carcinoma parental cell line and Nbs1 knockout (KO) HeLa cell line. PVDF membrane was probed with 1:1000 of Rabbit Anti-Human Polyclonal [NB100-143] followed by HRP-conjugated Anti-Rabbit IgG Secondary Antibody (HAF008). Specific band was detected for Nbs1 at approximately 95 kDa (as indicated) in the parental HeLa cell line, but is not detectable in the knockout HeLa cell line. This experiment was conducted under reducing conditions.")
![<b>Genetic Strategies Validation. </b>Western Blot: Nbs1 Antibody [NB100-143] - Western Blot with Nbs1 Antibody [NB100-143]. KSHV LANA recruits MRN (Mre11-Rad50-NBS1) complex. Co-immunoprecipitation of endogenous LANA and MRN proteins in BC3 cells. Cells were lysed using TBS-T buffer and the cell lysate was incubated with benzonase. After centrifugation, supernatant was incubated overnight with anti-LANA or IgG-control beads. The precipitated complexes were analyzed for the presence of endogenous Rad50, Mre11 and NBS1 by SDS-PAGE and immunoblotting. Image collected and cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.ppat.1006335), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/Nbs1-Antibody-Western-Blot-NB100-143-img0016.jpg)
![Immunocytochemistry/Immunofluorescence: Nbs1 Antibody [NB100-143] - ICC/IF analysis of Nbs1 in HeLa cells with Nbs1 Antibody [NB100-143]. Image from verified customer review.](http://images.novusbio.com/fullsize/Nbs1-Antibody-Immunocytochemistry-Immunofluorescence-NB100-143-img0011.jpg)
![Immunohistochemistry-Paraffin: Nbs1 Antibody [NB100-143] - FFPE human testis using Nbs1 antibody [NB100-143] at 1:200 on a Bond Rx autostainer (Leica Biosystems). The assay involved 20 minutes of heat induced antigen retrieval (HIER) using 10 mM sodium citrate buffer (pH 6.0) and endogenous peroxidase quenching with peroxide block. The sections were incubated with primary antibody for 30 minutes and Bond Polymer Refine Detection (Leica Biosystems) with DAB was used for signal development followed by counterstaining with hematoxylin. Whole slide scanning and capturing of representative images was performed using Aperio AT2 (Leica Biosystems). Staining was performed by Histowiz.](http://images.novusbio.com/fullsize/Nbs1-Antibody-Immunohistochemistry-Paraffin-NB100-143-img0014.jpg)
![Western Blot: Nbs1 Antibody [NB100-143] - Analysis of HeLa whole cell lysate [NB800-PC1] using rabbit polyclonal NBS1 antibody [NB100-143]. Observed Molecular Weight at ~95 kDa.](http://images.novusbio.com/fullsize/Nbs1-Antibody-Western-Blot-NB100-143-img0010.jpg)
![<b>Genetic Strategies Validation. </b>Western Blot: Nbs1 Antibody [NB100-143] - Detection of NBS1 in Human Bone Osteosarcoma Epithelial Cells (U2OS whole cell lysate) using Nbs1 Antibody [NB100-143] at a dilution of 1:1000. Specificity was confirmed using a siRNA anti-NBS1 (targeting sequence: GGAAGAAACGUGAACUCAA). Image provided by Sebastien Britton of the Institute of Pharmacology and Structural Biology.](http://images.novusbio.com/fullsize/Nbs1-Antibody-Western-Blot-NB100-143-img0012.jpg)
![Western Blot: Nbs1 Antibody [NB100-143] - Western Blot with Nbs1 Antibody [NB100-143]. TIG-1 human primary fibroblasts, whole cell lysate (30 ug). Image from verified customer review.](http://images.novusbio.com/fullsize/Nbs1-Antibody-Western-Blot-NB100-143-img0013.jpg)
![Immunocytochemistry/Immunofluorescence: Nbs1 Antibody [NB100-143] - Staining of HeLa cells using Nbs1 Antibody [NB100-143].](http://images.novusbio.com/fullsize/Nbs1-Antibody-Immunocytochemistry-Immunofluorescence-NB100-143-img0009.jpg)
![<b>Genetic Strategies Validation. </b>Immunocytochemistry/ Immunofluorescence: Nbs1 Antibody [NB100-143] - TOPBP1 recruitment in response to rDNA breaks. TOPBP1 localization 2 h after I-Ppo1 transfection in NBS1-delta-N cells and NBS1-delta-N cells complemented with wild-type and mutant NBS1-mNG (percentage of cells with > 2 TOPBP1 caps are indicated; one of two experiments is shown). Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31913317/) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/Nbs1 Antibody-Knockdown Validated-NB100-143-img0017.jpg)
![Immunocytochemistry/ Immunofluorescence: Nbs1 Antibody [NB100-143] - Replication centers of the integrated HPV recruit Mre11-Nbs1-Rad50 complex & Ku70/80 heterodimer.HeLa cells were transfected & analyzed as described previously. Co-immunostaining of HPV18 E1 (Alexa Fluor 568, second column) & the following proteins are presented: Mre11, Nbs1, Rad50, & Ku70/80 proteins (Alexa Fluor 488, first column). The localizations of the E1 & the respective DNA repair proteins are also shown in the third column as a merged image & DAPI stained nuclei are presented in the fourth column. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/19390600), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-143_rabbit-polyclonal-nbs1-antibody-310202415291962.jpg)
![Immunocytochemistry/ Immunofluorescence: Nbs1 Antibody [NB100-143] - Loss of MUS81 activates DNA damage responseA. MUS81 depleted U2OS cells accumulate NBS1 foci defining sites of DNA damage. B. Partial co-localization of NBS1 foci & RPA foci in MUS81-depleted cells. C. Co-localization of RPA foci to ssDNA regions. Cells were labelled with BrdU for 3 days concomitant with MUS81 depletion. BrdU was detected at ssDNA regions by immunofluorescence. D. NBS1 foci arise in cells that are both positive & negative for Cyclin A expression. Scale bars, 5 μm. E. NBS1 foci form largely at non-telomeric loci. F. Partial co-localization of NBS1 foci with PML nuclear bodies. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/26415217), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-143_rabbit-polyclonal-nbs1-antibody-310202415395910.jpg)
![Immunocytochemistry/ Immunofluorescence: Nbs1 Antibody [NB100-143] - Loss of MUS81 activates DNA damage responseA. MUS81 depleted U2OS cells accumulate NBS1 foci defining sites of DNA damage. B. Partial co-localization of NBS1 foci & RPA foci in MUS81-depleted cells. C. Co-localization of RPA foci to ssDNA regions. Cells were labelled with BrdU for 3 days concomitant with MUS81 depletion. BrdU was detected at ssDNA regions by immunofluorescence. D. NBS1 foci arise in cells that are both positive & negative for Cyclin A expression. Scale bars, 5 μm. E. NBS1 foci form largely at non-telomeric loci. F. Partial co-localization of NBS1 foci with PML nuclear bodies. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/26415217), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-143_rabbit-polyclonal-nbs1-antibody-310202415293317.jpg)
![Immunocytochemistry/ Immunofluorescence: Nbs1 Antibody [NB100-143] - Loss of MUS81 activates DNA damage responseA. MUS81 depleted U2OS cells accumulate NBS1 foci defining sites of DNA damage. B. Partial co-localization of NBS1 foci & RPA foci in MUS81-depleted cells. C. Co-localization of RPA foci to ssDNA regions. Cells were labelled with BrdU for 3 days concomitant with MUS81 depletion. BrdU was detected at ssDNA regions by immunofluorescence. D. NBS1 foci arise in cells that are both positive & negative for Cyclin A expression. Scale bars, 5 μm. E. NBS1 foci form largely at non-telomeric loci. F. Partial co-localization of NBS1 foci with PML nuclear bodies. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/26415217), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-143_rabbit-polyclonal-nbs1-antibody-31020241534354.jpg)
![Immunocytochemistry/ Immunofluorescence: Nbs1 Antibody [NB100-143] - Loss of MUS81 activates DNA damage responseA. MUS81 depleted U2OS cells accumulate NBS1 foci defining sites of DNA damage. B. Partial co-localization of NBS1 foci & RPA foci in MUS81-depleted cells. C. Co-localization of RPA foci to ssDNA regions. Cells were labelled with BrdU for 3 days concomitant with MUS81 depletion. BrdU was detected at ssDNA regions by immunofluorescence. D. NBS1 foci arise in cells that are both positive & negative for Cyclin A expression. Scale bars, 5 μm. E. NBS1 foci form largely at non-telomeric loci. F. Partial co-localization of NBS1 foci with PML nuclear bodies. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/26415217), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-143_rabbit-polyclonal-nbs1-antibody-31020241539451.jpg)
![Immunocytochemistry/ Immunofluorescence: Nbs1 Antibody [NB100-143] - HPV16 E2 partially colocalizes with the MRN complex proteins Mre11 & Nbs1. C33a cells were transfected with an HPV16 E2 expression plasmid, fixed in ice-cold methanol, & stained with an E2-specific antibody (green). DNA was stained with Hoechst 33342 (blue). (A) Endogenous Nbs1 was detected with an Nbs1-specific antibody (red/gray). (B) Endogenous Mre11 was detected with an Mre11-specific rabbit antibody (red/gray). Bar, 5 μm. Digital zoom is shown at the bottom. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28031358), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-143_rabbit-polyclonal-nbs1-antibody-310202415392545.jpg)
![Immunocytochemistry/ Immunofluorescence: Nbs1 Antibody [NB100-143] - Loss of MUS81 activates DNA damage responseA. MUS81 depleted U2OS cells accumulate NBS1 foci defining sites of DNA damage. B. Partial co-localization of NBS1 foci & RPA foci in MUS81-depleted cells. C. Co-localization of RPA foci to ssDNA regions. Cells were labelled with BrdU for 3 days concomitant with MUS81 depletion. BrdU was detected at ssDNA regions by immunofluorescence. D. NBS1 foci arise in cells that are both positive & negative for Cyclin A expression. Scale bars, 5 μm. E. NBS1 foci form largely at non-telomeric loci. F. Partial co-localization of NBS1 foci with PML nuclear bodies. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/26415217), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-143_rabbit-polyclonal-nbs1-antibody-310202415175283.jpg)
![Western Blot: Nbs1 Antibody [NB100-143] - UFL1 regulates the ATM signaling. a U2OS cells expressing UFL1 tet-on shRNA1 were irradiated with 2 Gy IR. Thirty minutes later, cells were lysed & blotted with indicated antibodies. b Representative picture of gamma H2AX, 53BP1, & BRCA1 foci in control (Dox-) & UFL1 knockdown (Dox+) U2OS cells 1 h after 0.5 Gy treatment. Scale bars, 10 µm. c–e Quantification of intensities of gamma H2AX, 53BP1, & BRCA1 foci in control (Dox-) & UFL1 knockdown (Dox+) U2OS cells. Data presented as mean ± SD of n = 50 cells. **p 100 cells. Error bars = SD. *** p-value <0.0001, unpaired two-tailed t-test.DOI://dx.doi.org/10.7554/eLife.07270.005Inhibition of oxidative stress reduces cell migration and invasion.ROS inhibitor NAC reduces cell migration to a similar extent as ATM-depletion. siATM and siNC control MDA-MB-231 cells were either untreated or treated with NAC and analyzed as in Figure 2D for cell migration. Right panel: Western blot of ATM depletion and quantification of cell migration for each sample.DOI://dx.doi.org/10.7554/eLife.07270.006 Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/26030852), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-143_rabbit-polyclonal-nbs1-antibody-knockdown-validated-13220261817564.jpg)
![Immunocytochemistry/Immunofluorescence: TRF-2 Antibody [NB110-57130] - HeLa cells were fixed for 10 minutes using 10% formalin and then permeabilized for 5 minutes using 1X TBS + 0.5% Triton X-100. The cells were incubated with antibody at a 1:200 dilution overnight at 4 degrees Celsius and detected with DyLight 488 (Green) at a 1:500 dilution. Alpha tubulin was used as a co-stain at a 1:1000 dilution and detected with Dylight 550 (Red). Nuclei were detected with DAPI (Blue) at 2.0 ug/ml in 1X PBS. Cells were imaged using a 40X objective.](http://images.novusbio.com/fullsize/TRF-2-Antibody-Immunocytochemistry-Immunofluorescence-NB110-57130-img0011.jpg "Immunocytochemistry/Immunofluorescence: TRF-2 Antibody [NB110-57130] - HeLa cells were fixed for 10 minutes using 10% formalin and then permeabilized for 5 minutes using 1X TBS + 0.5% Triton X-100. The cells were incubated with antibody at a 1:200 dilution overnight at 4 degrees Celsius and detected with DyLight 488 (Green) at a 1:500 dilution. Alpha tubulin was used as a co-stain at a 1:1000 dilution and detected with Dylight 550 (Red). Nuclei were detected with DAPI (Blue) at 2.0 ug/ml in 1X PBS. Cells were imaged using a 40X objective.")
![Simple Western: TRF-2 Antibody [NB110-57130] - Lane view shows a specific band for TRF2 in 1.0 mg/mL of HeLa lysate. This experiment was performed under reducing conditions using the 12-230 kDa separation system.](http://images.novusbio.com/fullsize/TRF-2-Antibody-Simple-Western-NB110-57130-img0010.jpg)
![Western Blot: TRF-2 Antibody [NB110-57130] - Analysis of HeLa whole cell lysate (A), HeLa nuclear cell lysate (B), k562 cell lysate (C), HepG2 cell lysate (D), NIH/3T3 cell lysate (E), CHO cell lysate (F), PC12 cell lysate (G), and Cos7 cell lysate (H) using antibody at a concentration of 2 ug/mL.](http://images.novusbio.com/fullsize/TRF-2-Antibody-Western-Blot-NB110-57130-img0008.jpg)
![Immunohistochemistry-Paraffin: TRF-2 Antibody [NB110-57130] - Analysis in xenografted human breast cancer tissue using DAB with hematoxylin counterstain.](http://images.novusbio.com/fullsize/TRF-2-Antibody-Immunohistochemistry-Paraffin-NB110-57130-img0007.jpg)
![Immunohistochemistry-Paraffin: TRF-2 Antibody [NB110-57130] - Analysis of FFPE human breast cancer tissue with rabbit polyclonal TRF2 antibody at a dilution of 1:200. The staining was developed with HRP-DAB detection method and the counterstaining was performed using hematoxylin. This TRF2 antibody generated an expected nuclear signal in all the cancer cells and the stromal cells. In the tested section, only a subset of myoepithelial cells showed positivity for this protein.](http://images.novusbio.com/fullsize/TRF-2-Antibody-Immunohistochemistry-Paraffin-NB110-57130-img0013.jpg)
![Immunocytochemistry/Immunofluorescence: TRF-2 Antibody [NB110-57130] - NIH3T3 cells were fixed in 4% paraformaldehyde for 10 minutes and permeabilized in 0.5% Triton X-100 in PBS for 5 minutes. The cells were incubated with anti-TRF-2 Antibody NB110-57130 at 2 ug/ml overnight at 4C and detected with an anti-rabbit Dylight 488 (Green) at a 1:1000 dilution for 60 minutes. Nuclei were counterstained with DAPI (Blue). Cells were imaged using a 100X objective and digitally deconvolved.](http://images.novusbio.com/fullsize/TRF-2-Antibody-Immunocytochemistry-Immunofluorescence-NB110-57130-img0016.jpg)
![Flow Cytometry: TRF-2 Antibody [NB110-57130] - An intracellular stain was performed on HeLa cells with TRF-2 Antibody NB110-57130 (blue) and a matched isotype control NBP2-24891 (orange). Cells were fixed with 4% PFA and then permeabilized with 0.1% saponin. Cells were incubated in an antibody dilution of 1.0 ug/mL for 30 minutes at room temperature, followed by Rabbit IgG (H+L) Cross-Adsorbed Secondary Antibody, Dylight 550 (SA5-10033, Thermo Fisher).](http://images.novusbio.com/fullsize/TRF-2-Antibody-Flow-Cytometry-NB110-57130-img0017.jpg)
![Chromatin Immunoprecipitation: TRF-2 Antibody [NB110-57130] - Analysis in mouse. Titrated TRF2 antibody to determine concentration required for ChIP experiment. ChIP image submitted by a verified customer review.](http://images.novusbio.com/fullsize/TRF-2-Antibody-Chromatin-Immunoprecipitation-NB110-57130-img0009.jpg)
![<b>Genetic Strategies Validation. </b>Immunocytochemistry/Immunofluorescence: TRF-2 Antibody [NB110-57130] - RNAi-mediated depletion of human separase (ESPL1) induces TIFs. Control scrambled siRNA- (control) and ESPL1 siRNA-treated fibroblasts stained with anti-p53-binding protein 1 (53BP1; green) and anti-TRF2 (red). It is noteworthy that in ESPL1 siRNA-treated cells, 53BP1 signals frequently overlap with TRF2 signals marking the TIFs. Scale bar, 5 um. Image collected and cropped by CiteAb from the following publication (//www.nature.com/doifinder/10.1038/ncomms10405), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/TRF-2-Antibody-Immunocytochemistry-Immunofluorescence-NB110-57130-img0015.jpg)
![Immunohistochemistry-Paraffin: TRF-2 Antibody [NB110-57130] - Analysis of FFPE human breast cancer tissue with rabbit polyclonal TRF2 antibody at 1:200 dilution. The staining was developed with HRP-DAB detection method and the counterstaining was performed using hematoxylin. This TRF2 antibody generated an expected nuclear signal in all the cancer cells and the stromal cells. In the tested section, only a subset of myoepithelial cells showed positivity for this protein.](http://images.novusbio.com/fullsize/TRF-2-Antibody-Immunohistochemistry-Paraffin-NB110-57130-img0012.jpg)
![Flow Cytometry: TRF-2 Antibody [NB110-57130] - An intracellular stain was performed on HeLa cells with TRF-2 Antibody NB110-57130AF488 (blue) and a matched isotype control (orange). Cells were fixed with 4% PFA and then permeabilized with 0.1% saponin. Cells were incubated in an antibody dilution of 5 ug/mL for 30 minutes at room temperature. Both antibodies were conjugated to Alexa Fluor 488.](http://images.novusbio.com/fullsize/TRF-2-Antibody-Flow-Cytometry-NB110-57130-img0014.jpg)
![Western Blot: TRF-2 Antibody - BSA Free [NB110-57130] - Repressive chromatin induced on p21 promoter in TRF2 dependent way. (A–C) Loss of chromatin activation marks H3K4Me, H3K4Me2 in stable TRF2 expressed HT1080 cells (A); increase in LSD1 occupancy in TRF2 over-expressing HT1080 cells. (B) (Full images are shown in Supplementary Figures S6 & S7); Co-immunoprecipitation of TRF2 with LSD1 (immunoprecipitation with anti-TRF2 antibody followed by immunoblotting with anti-LSD1 or anti-TRF2 antibody) (C); (D) Reverse Co-immunoprecipitation of LSD1 with TRF2 (immunoprecipitation with anti-LSD1 antibody followed by immunoblotting with anti-TRF2 antibody); (E) & reduced occupancy of the repressor complex REST, Co-REST & LSD1 on silencing TRF2 on p21 promoter. Image collected & cropped by CiteAb from the following publication (//www.nature.com/articles/s41598-017-11177-1), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-57130_rabbit-polyclonal-trf-2-antibody-31020241528452.jpg)
![Chromatin Immunoprecipitation: TRF-2 Antibody - BSA Free [NB110-57130] - TRF2 occupancy on G4-motif sites on gene promoters within cells.A, telomeric enrichment was tested for TRF2 ChIP samples performed in HT1080 cells. Telomeric signal was normalized to signal from ALU probe. B, TRF2 occupancy at gene promoter sites in HT1080 cells (endogenous TRF2 & TRF2-overexpressed) quantified using ChIP-qRT PCR. TRF2 ChIP/IgG (mock) enrichment was normalized to 1% input; CTCF promoter (which does not harbor a TRF2 peak) was used as negative control; error bars correspond to S.D., & statistical significance was calculated by paired t test (*, p < 0.05; **, p < 0.01). For the TRF2-overexpressed condition (in red), all p values were <0.01. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31575660), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-57130_rabbit-polyclonal-trf-2-antibody-310202415293320.jpg)
![Western Blot: TRF-2 Antibody - BSA Free [NB110-57130] - Repressive chromatin induced on p21 promoter in TRF2 dependent way. (A–C) Loss of chromatin activation marks H3K4Me, H3K4Me2 in stable TRF2 expressed HT1080 cells (A); increase in LSD1 occupancy in TRF2 over-expressing HT1080 cells. (B) (Full images are shown in Supplementary Figures S6 & S7); Co-immunoprecipitation of TRF2 with LSD1 (immunoprecipitation with anti-TRF2 antibody followed by immunoblotting with anti-LSD1 or anti-TRF2 antibody) (C); (D) Reverse Co-immunoprecipitation of LSD1 with TRF2 (immunoprecipitation with anti-LSD1 antibody followed by immunoblotting with anti-TRF2 antibody); (E) & reduced occupancy of the repressor complex REST, Co-REST & LSD1 on silencing TRF2 on p21 promoter. Image collected & cropped by CiteAb from the following publication (//www.nature.com/articles/s41598-017-11177-1), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-57130_rabbit-polyclonal-trf-2-antibody-310202415363710.jpg)
![Chromatin Immunoprecipitation: TRF-2 Antibody - BSA Free [NB110-57130] - Thousands of extra-telomeric TRF2 binding sites found across the genome.A, extra-telomeric TRF2 peaks found in HT1080 cells following TRF2 ChIP-Seq: 20304 TRF2 peaks were common between two independent experiments. B, distribution of common TRF2 peaks around TSSs. Distance from the TSS is shown in kb. C, replicate consistency plot generated using irreproducible discovery rate analysis; 1956 peaks found at ≤0.01 are marked. D, distribution of 1956 TRF2 peaks with IDR 0.01 (TRF2HC peaks) around the TSS. Distance from the TSS is shown in kb. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31575660), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-57130_rabbit-polyclonal-trf-2-antibody-310202415371955.jpg)
![Western Blot: TRF-2 Antibody - BSA Free [NB110-57130] - TRF1HP1 alpha allele-specific protection effects upon si-TRF2-induced telomeric damage. 72 h after transfection, a TRF2 knockdown efficiency with antibody against TRF2 (anti-TRF2) & GAPDH (anti-GAPDH) as loading control. (−) si-non-targeting; (+) si-TRF2. Quantification of TIFs in b si-non-targeting (n = 32–47 nuclei per group) or c si-TRF2. Left *p = 0.0188, right *p = 0.0192, **p = 0.0042, ****p < 0.0001 (n = 31–48 nuclei per group). b, c Significance is assessed by one-way ANOVA & Dunnett’s multiple comparison test with 95% confidence level. Error bars represent s.e.m. Note the similar pattern among TRF1HP1 alpha alleles in c compared to the corresponding allele pattern in Fig. 4b Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30181605), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-57130_rabbit-polyclonal-trf-2-antibody-310202415284520.jpg)
![Chromatin Immunoprecipitation: TRF-2 Antibody - BSA Free [NB110-57130] - TRF2 peaks harbor G-quadruplex motifs genome-wide.A, schematic representation of a G4 motif; sequence pattern with loop/stem & PG4 motif formed by a tetrad of guanine trimers interspersed with loops that can vary in length. B & C, PG4 motifs & TRF2 peaks significantly overlap. High-confidence TRF2-binding sites (TRF2HC peaks) determined by ChIP-Seq in HT1080 cells were significantly enriched in PG4-motif sequences (B), & conversely, PG4-motif sequences were enriched within TRF2HC peaks (C). Nonoverlapping PG4 motifs were considered for analysis; for control analysis, 100 regions of identical length for each TRF2 peak were taken. *, p < 0.05; **, p < 0.01 (Fisher's exact test). Error bars, S.D. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31575660), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-57130_rabbit-polyclonal-trf-2-antibody-31020241538415.jpg)
![Western Blot: TRF-2 Antibody - BSA Free [NB110-57130] - Repressive chromatin induced on p21 promoter in TRF2 dependent way. (A–C) Loss of chromatin activation marks H3K4Me, H3K4Me2 in stable TRF2 expressed HT1080 cells (A); increase in LSD1 occupancy in TRF2 over-expressing HT1080 cells. (B) (Full images are shown in Supplementary Figures S6 & S7); Co-immunoprecipitation of TRF2 with LSD1 (immunoprecipitation with anti-TRF2 antibody followed by immunoblotting with anti-LSD1 or anti-TRF2 antibody) (C); (D) Reverse Co-immunoprecipitation of LSD1 with TRF2 (immunoprecipitation with anti-LSD1 antibody followed by immunoblotting with anti-TRF2 antibody); (E) & reduced occupancy of the repressor complex REST, Co-REST & LSD1 on silencing TRF2 on p21 promoter. Image collected & cropped by CiteAb from the following publication (//www.nature.com/articles/s41598-017-11177-1), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-57130_rabbit-polyclonal-trf-2-antibody-310202415392522.jpg)
![Western Blot: TRF-2 Antibody - BSA Free [NB110-57130] - TRF2 transcriptionally regulates p21 expression through promoter occupancy. (A) Quantitative ChIP using TRF2 antibody gives enriched binding of TRF2 on p21 promoter in HT1080 & MDA-MB-231 cells, IgG was used as isotypic antibody control; normalized with 10% input (data represented as mean ± SEM, for three replicates). (B,C) TRF2 represses p21 promoter activity. In luciferase assay, si-RNA-mediated silencing or TRF2 over expression resulted in increased (B, *p value < 0.05, Student’s t-test; data represented as mean ± SEM of three replicates) or reduction (C, *p value < 0.05, Student’s t-test; data represented as mean ± SEM of three replicates) in p21 promoter activity in HT1080 & MDA-MB-231 cells, respectively; over expression of TRF2 devoid of DNA binding [deletion of basic (delB), myb (delM) & both basic/myb (delB-delM) domains] resulted in partial or complete rescue of p21 promoter activity in HT1080 & MDA-MB-231 cells (data represented as mean ± SEM, for three replicates) (C). (D,E) HT1080 cells over expressing TRF2 show reduced p21 protein expression, bar graph shows the densitometry analysis of three different immunoblot replicates (*p value < 0.05, Student’s t-test; data represented as mean ± SEM of three replicates). (E) (Full images are shown in Supplementary Figure S5); TRF2 silencing results in increase in p21 protein, bar graph shows the densitometry analysis of three different immunoblots (*p value < 0.05, Student’s t-test; data represented as mean ± SEM of three replicates) (F); & mRNA expression in HT1080 cells (*p value < 0.05, Student’s t-test; data represented as mean ± SEM of three replicates, GAPDH used as internal control for real-time PCR). Image collected & cropped by CiteAb from the following publication (//www.nature.com/articles/s41598-017-11177-1), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-57130_rabbit-polyclonal-trf-2-antibody-31020241624926.jpg)
![Chromatin Immunoprecipitation: TRF-2 Antibody - BSA Free [NB110-57130] - TRF2 occupancy at gene promoters is sensitive to intracellular G-quadruplex–binding ligand 360A.A, TRF2 occupancy at gene promoter sites was checked by ChIP qRT-PCR in HT1080 cells following overexpression of TRF2 in the presence or absence of 360A. Error bars, S.D. from three independent experiments; CTCF promoter was used as a negative control. B, TRF2 level was checked by Western blotting in the presence of the ligand 360A in both untransfected & TRF2 transient overexpression conditions. Overexpression was also confirmed by probing for DDK tag. GAPDH was used as loading control. C, expression of target genes was analyzed by qRT-PCR in HT1080 cells following overexpression of TRF2 in the presence or absence of 360A. GAPDH expression was used for normalization; error bars, S.D. from three independent experiments. Statistical significance was calculated by paired t test (*, p < 0.05; **, p < 0.01). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31575660), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-57130_rabbit-polyclonal-trf-2-antibody-3102024162491.jpg)
![Western Blot: TRF-2 Antibody - BSA Free [NB110-57130] - A. Co-IP analysis of the interaction between DSP & TRF2 in HEK293 cells & MCF-7 cells. B. Co-IP analysis of the interaction between DSP & TRF2 in DSP-EGFP transfected HEK293 cells or DSP△NLS-EGFP transfected HEK293 cells. C. DSP pull down by telomere targeting CASID with the condition of TRF2 knockdown in HEK293 cells. Histone H3 is the loading control. D.TRF1 & TRF2 pull-down assay by telomere targeting CASID with the condition of DSP knockdown in HEK293 cells. E. Left, Dot blot of telomere DNA repeats in chromatin pull down by DSP with the condition of TRF1 or TRF2 knockdown. The dot-blot was performed at least three times & the represented one is shown. Right, the histogram shows the quantitated results of the dot blots. The triple asterisks (***) indicates a p-value less than 0.01. ns. indicates the insignificance difference. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31595153), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-57130_rabbit-polyclonal-trf-2-antibody-310202416235527.jpg)
![Immunocytochemistry/ Immunofluorescence: TRF-2 Antibody - BSA Free [NB110-57130] - TERRA & telomere transcription in ALT cells.(a) TERRA northern blot hybridizations of RNA from the indicated cell lines (VA13: WI-38 VA13; 1.2.11: HeLa 1.2.11) pre-treated with RNaseA or left untreated. Ethidium bromide stained 18S ribosomal RNA (rRNA) is shown to control for loading. Long TERRA molecules comprised between the wells of the gels (w) & 28S rRNA are indicated. (b) TERRA CpG-island promoter methylation analysis of the indicated cell lines. Genomic DNA was digested with the methylation sensitive restriction enzyme MspI or its methylation insensitive isoschizomer HpaII. DNA was hybridized using a radioactively labelled probe detecting TERRA promoter CpG-island repeats. Nomet: fragments corresponding to unmethylated restriction products. (c) Dot blot hybridization of DNA immunoprecipitated with antibodies against phosphorylated Serines S2 & S5 of RNA polymerase II C-terminal domain. Hybridizations were performed with a telomeric probe. Quantifications are shown at the bottom. (d) Bars & error bars are averages & s.d. from three independent experiments. (e) Examples of TERRA FISH in the indicated cells. TERRA is shown in red, DAPI-stained DNA in blue. Scale bar, 9 μm. (f) IF/FISH experiments in the indicated cell lines. TERRA is in red, TRF2 in green & PML in blue. In the merge panels, arrowheads point to nuclear foci where the three factors co-localize. Scale bar, 9 μm. (g) Information surface at 0.01 μm detail level of three TERRA-containing APBs. TERRA is in red, TRF2 in green & PML in cyan. Images were generated with Three-Dimensional Structured Illumination Microscopy (3D-SIM). Scale bars, 0.4 μm. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/25330849), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-57130_rabbit-polyclonal-trf-2-antibody-310202416235545.jpg)
![Western Blot: TRF-2 Antibody - BSA Free [NB110-57130] - TRF2 occupancy at gene promoters is sensitive to intracellular G-quadruplex–binding ligand 360A.A, TRF2 occupancy at gene promoter sites was checked by ChIP qRT-PCR in HT1080 cells following overexpression of TRF2 in the presence or absence of 360A. Error bars, S.D. from three independent experiments; CTCF promoter was used as a negative control. B, TRF2 level was checked by Western blotting in the presence of the ligand 360A in both untransfected & TRF2 transient overexpression conditions. Overexpression was also confirmed by probing for DDK tag. GAPDH was used as loading control. C, expression of target genes was analyzed by qRT-PCR in HT1080 cells following overexpression of TRF2 in the presence or absence of 360A. GAPDH expression was used for normalization; error bars, S.D. from three independent experiments. Statistical significance was calculated by paired t test (*, p < 0.05; **, p < 0.01). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31575660), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-57130_rabbit-polyclonal-trf-2-antibody-31020241624924.jpg)
![Western Blot: TRF-2 Antibody - BSA Free [NB110-57130] - A. Gene ontology analysis of proteins identified by CASID targeting telomeres. B. Western blot detection of TRF1, POT1, & DSP in the proteins pulled down by CASID with the presence of telo-sgRNA in HEK293 cells. Input represents the initial nuclear extract before the pull-down mediated by CASID. C. left, ChIP assay of telomere binding of TRF2 or DSP in MCF-7 cells & HEK293 cells. The chromatin DNA precipitated by anti-DSP & anti-TRF2 antibodies were analyzed by dot blot using the probes recognizing telomere (Telo-p) or Alu DNA repeats (Alu-p). The detection of Alu DNA repeats serves as negative control. The dot-blot was performed at least three times & the represented one is shown. Right, the histogram shows the quantitated results of the dot blots. The triple asterisks (***) indicates a p-value less than 0.01. D. Fluorescence imaging of DSP-EGFP in MCF-7 cells & U2OS cells. The EGFP signal indicates the localization of DSP-EGFP (green) & the Telo-FISH signal indicates the localization of telomeres (red). The overlapping between DSP-EGFP & Telo-FISH is in yellow as revealed in the enlarged nuclear area. The dCAS9-EGFP construct without telo-sgRNA was used for U2OS transfection & the imaging of EGFP serves as negative control. E. DSP localization in interphase & pro-metaphase nucleus. DSP-EGFP indicates the DSP locations & DAPI indicates the nucleus. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31595153), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-57130_rabbit-polyclonal-trf-2-antibody-31020241624912.jpg)
![Western Blot: TRF-2 Antibody - BSA Free [NB110-57130] - TRF2 interacts with lamin A/C.(a) Pull down of endogenous TRF2 in IMR90s. The top panel shows a blot probed for endogenous lamin A/C, & the bottom panel shows a blot with the same samples probed for TRF2. (b) Pull down of endogenously expressed lamin A/C in IMR90s. The top panel shows a blot probed for endogenous TRF2, & the bottom panel shows a blot with the same samples probed for endogenous lamin A/C. (c) Pull down of endogenous lamin A/C in IMR90s exogenously expressing GFP, GFP-TRF2, GFP-TRF delta B delta M or GFP-TRF1. The top panel shows a blot probed for GFP, & the bottom panel shows the same blot probed for lamin A/C. (d) Pull down of endogenous TRF2 in IMR90s exogenously expressing GFP, GFP-LMNA or progerin (GFP-LMNA delta 50). The top panel shows a blot probed for GFP, & the bottom panel shows the same blot probed for TRF2. Asterisks denote IgG bands. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/25399868), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-57130_rabbit-polyclonal-trf-2-antibody-310202416235540.jpg)
![Western Blot: TRF-2 Antibody - BSA Free [NB110-57130] - Widespread dysregulation of shelterin protein expression in bortezomib-treated HEL & BGC-823 cellsA. & B. mRNA levels of shelterin factors TRF1, TRF2, TPP1, POT1, RAP1 & TIN2 in bortezomib-treated cells. Cells were treated with bortezomib for 24 hours & qPCR was used for quantitative assays. The levels of each target mRNA in bortezomib-treated cells were expressed as percentages of those in untreated cells. (A) HEL cells & (B) BGC-823 cells. C. & D. Immunoblotting assessment of TRF1, TRF2 & POT1 protein expression in bortezomib-treated cells. Same sets of cells above were analyzed for TRF1, TRF2 & POT1 protein levels & shown was representative of three independent experiments. (C) HEL cells & (D) BGC-823 cells. * & **: P < 0.05 & 0.01, respectively. BTZ, bortezomib. Image collected & cropped by CiteAb from the following publication (//www.oncotarget.com/lookup/doi/10.18632/oncotarget.5752), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-57130_rabbit-polyclonal-trf-2-antibody-31020241623553.jpg)
![Western Blot: TRF-2 Antibody - BSA Free [NB110-57130] - A. Co-IP analysis of the interaction between DSP & TRF2 in HEK293 cells & MCF-7 cells. B. Co-IP analysis of the interaction between DSP & TRF2 in DSP-EGFP transfected HEK293 cells or DSP△NLS-EGFP transfected HEK293 cells. C. DSP pull down by telomere targeting CASID with the condition of TRF2 knockdown in HEK293 cells. Histone H3 is the loading control. D.TRF1 & TRF2 pull-down assay by telomere targeting CASID with the condition of DSP knockdown in HEK293 cells. E. Left, Dot blot of telomere DNA repeats in chromatin pull down by DSP with the condition of TRF1 or TRF2 knockdown. The dot-blot was performed at least three times & the represented one is shown. Right, the histogram shows the quantitated results of the dot blots. The triple asterisks (***) indicates a p-value less than 0.01. ns. indicates the insignificance difference. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31595153), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-57130_rabbit-polyclonal-trf-2-antibody-31020241624919.jpg)
![Western Blot: TRF-2 Antibody - BSA Free [NB110-57130] - Telomere deprotection contributes to replication stress lethality. a Western blots of whole cell extracts from HT1080 6TG cells stably transduced with control, TRF2 shRNA (TRF sh-F) or TRF2 over expression (TRF2OE) vectors. b Representative images of cyto-centrifuged chromosome spreads stained with DAPI (blue), gamma -H2AX IF (red) & telomere PNA (green) from control, TRF sh-F or TRF2OE HT1080 6TG cells treated with DMSO or APH. Scale bar represents 10 µm. c, d Quantitation of mitotic telomere DDR foci from Control sh & TRF2 sh-F cells (c) or vector & TRF2OE cells (d) ± DMSO or APH (three biological replicates scoring n = 50 mitotic spreads per replicate compiled in a Tukey box plot, Mann–Whitney test). e Difference in the mean number of mitotic telomeric gamma -H2AX foci between HT1080 6TG TRF2 sh-F or TRF2OE cells & their appropriate vector control. These are a different representation of the same data shown in (c, d) (mean ± s.e.m., n = 3 three biological replications, Student’s t-test). f Mitotic duration to cell death in APH treated control, TRF2 sh-F & or TRF2OE cells (three biological replicates scoring ≥267 mitotic death events per condition are shown in a dot plot, mean ± s.e.m., Mann–Whitney test). g Mitotic outcome of control, TRF2 sh-F & TRF2OE cells treated with APH or DMSO (mean ± s.e.m., n = 3 biological replicates of at least 267 mitoses per condition, Fisher’s Exact Test). For all panels, *p < 0.05, **p < 0.01. Source data are provided as a Source Data file Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31530811), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-57130_rabbit-polyclonal-trf-2-antibody-310202416235510.jpg)
![Western Blot: TRF-2 Antibody - BSA Free [NB110-57130] - A. Co-IP analysis of the interaction between DSP & TRF2 in HEK293 cells & MCF-7 cells. B. Co-IP analysis of the interaction between DSP & TRF2 in DSP-EGFP transfected HEK293 cells or DSP△NLS-EGFP transfected HEK293 cells. C. DSP pull down by telomere targeting CASID with the condition of TRF2 knockdown in HEK293 cells. Histone H3 is the loading control. D.TRF1 & TRF2 pull-down assay by telomere targeting CASID with the condition of DSP knockdown in HEK293 cells. E. Left, Dot blot of telomere DNA repeats in chromatin pull down by DSP with the condition of TRF1 or TRF2 knockdown. The dot-blot was performed at least three times & the represented one is shown. Right, the histogram shows the quantitated results of the dot blots. The triple asterisks (***) indicates a p-value less than 0.01. ns. indicates the insignificance difference. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31595153), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-57130_rabbit-polyclonal-trf-2-antibody-31020241624913.jpg)
![Western Blot: TRF-2 Antibody - BSA Free [NB110-57130] - A. TRF2 or DSP1 pull down by telomere targeting CASID with the condition of MST-312 treatment (left) or hTERT knockdown (right) in MDA-MB-231cells. B. Southern blot of telomere DNA from MDA-MB-231cells treated with MST-312 or with hTERT knockdown. C. Top, Dot blot of telomere DNA repeats from the chromatin pull down by DSP from the cells treated by MST-312 (left) or hTERT knockdown (right). Alu DNA repeats serve as negative control. Bottom, the histogram shows the quantitated results of the dot blots. The triple asterisks (***) indicates a p-value less than 0.01. D. Fluorescence image of DSP-EGFP transfected MDA-MB-231 cells with the conditions of MST-312 treatment or hTERT knockdown. E. Pull down assay of DSP by CASID targeting telomere in WI38 cells with or without ectopically expression of hTERT gene. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31595153), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-57130_rabbit-polyclonal-trf-2-antibody-31020241624911.jpg)
![Western Blot: TRF-2 Antibody - BSA Free [NB110-57130] - Attenuation of bortezomib-induced shelterin protein dysregulation by hTERT over-expressionA. & B. Cells expressing ectopic hTERT were treated with bortezomib for 24 hours & mRNA levels of shelterin proteins then analyzed using qPCR. The levels of each target mRNA in bortezomib-treated cells were expressed as percentages of those in untreated cells. (A) HEL-hTERT cells & (B) BGC-823-hTERT cells. C. & D. Immunoblotting assessment of TRF1, TRF2 & POT1 protein expression in bortezomib-treated cells. Same sets of cells above were analyzed for TRF1, TRF2 & POT1 protein levels & shown was representative of three independent experiments. (C) HEL-hTERT cells & (D) BGC-823-hTERT cells.* & **: P < 0.05 & 0.01, respectively. BTZ, bortezomib. Image collected & cropped by CiteAb from the following publication (//www.oncotarget.com/lookup/doi/10.18632/oncotarget.5752), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-57130_rabbit-polyclonal-trf-2-antibody-310202416235549.jpg)
![Immunocytochemistry/ Immunofluorescence: TRF-2 Antibody - BSA Free [NB110-57130] - RNaseH1 depletion leads to RPA activation at ALT telomeres.(a) HeLa & U2OS cells were transfected with the indicated siRNAs & 48 & 72 h later protein extracts were prepared. Western blot analysis was performed using antibodies against RNaseH1, RPA32 phosphorylated at Serine 33 (pSer33), total RPA32 & KAP1 (loading control). The asterisk indicates a cross-reacting band. Cells treated for 6 h with 5 mM hydroxyurea (HU) were used as controls for pSer33 activation. (b) SiRNA transfected cells were subjected to indirect immunofluorescence using antibodies against TRF2 (to visualize telomeres; red) & pSer33 (green). DNA was counterstained with DAPI (blue). Arrows point to examples of pSer33 foci co-localizing with TRF2 (TIFs). Scale bar, 9 μm. Cells treated for 6 h with 5 mM HU were used as controls for pSer33 activation. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/25330849), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-57130_rabbit-polyclonal-trf-2-antibody-310202416235532.jpg)
![Western Blot: TRF-2 Antibody - BSA Free [NB110-57130] - TRF2 interacts with lamin A/C.(a) Pull down of endogenous TRF2 in IMR90s. The top panel shows a blot probed for endogenous lamin A/C, & the bottom panel shows a blot with the same samples probed for TRF2. (b) Pull down of endogenously expressed lamin A/C in IMR90s. The top panel shows a blot probed for endogenous TRF2, & the bottom panel shows a blot with the same samples probed for endogenous lamin A/C. (c) Pull down of endogenous lamin A/C in IMR90s exogenously expressing GFP, GFP-TRF2, GFP-TRF delta B delta M or GFP-TRF1. The top panel shows a blot probed for GFP, & the bottom panel shows the same blot probed for lamin A/C. (d) Pull down of endogenous TRF2 in IMR90s exogenously expressing GFP, GFP-LMNA or progerin (GFP-LMNA delta 50). The top panel shows a blot probed for GFP, & the bottom panel shows the same blot probed for TRF2. Asterisks denote IgG bands. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/25399868), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-57130_rabbit-polyclonal-trf-2-antibody-31020241624921.jpg)
![Western Blot: TRF-2 Antibody - BSA Free [NB110-57130] - Widespread dysregulation of shelterin protein expression in bortezomib-treated HEL & BGC-823 cellsA. & B. mRNA levels of shelterin factors TRF1, TRF2, TPP1, POT1, RAP1 & TIN2 in bortezomib-treated cells. Cells were treated with bortezomib for 24 hours & qPCR was used for quantitative assays. The levels of each target mRNA in bortezomib-treated cells were expressed as percentages of those in untreated cells. (A) HEL cells & (B) BGC-823 cells. C. & D. Immunoblotting assessment of TRF1, TRF2 & POT1 protein expression in bortezomib-treated cells. Same sets of cells above were analyzed for TRF1, TRF2 & POT1 protein levels & shown was representative of three independent experiments. (C) HEL cells & (D) BGC-823 cells. * & **: P < 0.05 & 0.01, respectively. BTZ, bortezomib. Image collected & cropped by CiteAb from the following publication (//www.oncotarget.com/lookup/doi/10.18632/oncotarget.5752), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-57130_rabbit-polyclonal-trf-2-antibody-310202416235531.jpg)
![Western Blot: TRF-2 Antibody - BSA Free [NB110-57130] - TRF2 interacts with lamin A/C.(a) Pull down of endogenous TRF2 in IMR90s. The top panel shows a blot probed for endogenous lamin A/C, & the bottom panel shows a blot with the same samples probed for TRF2. (b) Pull down of endogenously expressed lamin A/C in IMR90s. The top panel shows a blot probed for endogenous TRF2, & the bottom panel shows a blot with the same samples probed for endogenous lamin A/C. (c) Pull down of endogenous lamin A/C in IMR90s exogenously expressing GFP, GFP-TRF2, GFP-TRF delta B delta M or GFP-TRF1. The top panel shows a blot probed for GFP, & the bottom panel shows the same blot probed for lamin A/C. (d) Pull down of endogenous TRF2 in IMR90s exogenously expressing GFP, GFP-LMNA or progerin (GFP-LMNA delta 50). The top panel shows a blot probed for GFP, & the bottom panel shows the same blot probed for TRF2. Asterisks denote IgG bands. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/25399868), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-57130_rabbit-polyclonal-trf-2-antibody-3102024162490.jpg)
![Western Blot: TRF-2 Antibody - BSA Free [NB110-57130] - TRF2 transcriptionally regulates p21 expression through promoter occupancy. (A) Quantitative ChIP using TRF2 antibody gives enriched binding of TRF2 on p21 promoter in HT1080 & MDA-MB-231 cells, IgG was used as isotypic antibody control; normalized with 10% input (data represented as mean ± SEM, for three replicates). (B,C) TRF2 represses p21 promoter activity. In luciferase assay, si-RNA-mediated silencing or TRF2 over expression resulted in increased (B, *p value < 0.05, Student’s t-test; data represented as mean ± SEM of three replicates) or reduction (C, *p value < 0.05, Student’s t-test; data represented as mean ± SEM of three replicates) in p21 promoter activity in HT1080 & MDA-MB-231 cells, respectively; over expression of TRF2 devoid of DNA binding [deletion of basic (delB), myb (delM) & both basic/myb (delB-delM) domains] resulted in partial or complete rescue of p21 promoter activity in HT1080 & MDA-MB-231 cells (data represented as mean ± SEM, for three replicates) (C). (D,E) HT1080 cells over expressing TRF2 show reduced p21 protein expression, bar graph shows the densitometry analysis of three different immunoblot replicates (*p value < 0.05, Student’s t-test; data represented as mean ± SEM of three replicates). (E) (Full images are shown in Supplementary Figure S5); TRF2 silencing results in increase in p21 protein, bar graph shows the densitometry analysis of three different immunoblots (*p value < 0.05, Student’s t-test; data represented as mean ± SEM of three replicates) (F); & mRNA expression in HT1080 cells (*p value < 0.05, Student’s t-test; data represented as mean ± SEM of three replicates, GAPDH used as internal control for real-time PCR). Image collected & cropped by CiteAb from the following publication (//www.nature.com/articles/s41598-017-11177-1), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-57130_rabbit-polyclonal-trf-2-antibody-310202416235546.jpg)
![Western Blot: TRF-2 Antibody - BSA Free [NB110-57130] - TRF2 transcriptionally regulates p21 expression through promoter occupancy. (A) Quantitative ChIP using TRF2 antibody gives enriched binding of TRF2 on p21 promoter in HT1080 & MDA-MB-231 cells, IgG was used as isotypic antibody control; normalized with 10% input (data represented as mean ± SEM, for three replicates). (B,C) TRF2 represses p21 promoter activity. In luciferase assay, si-RNA-mediated silencing or TRF2 over expression resulted in increased (B, *p value < 0.05, Student’s t-test; data represented as mean ± SEM of three replicates) or reduction (C, *p value < 0.05, Student’s t-test; data represented as mean ± SEM of three replicates) in p21 promoter activity in HT1080 & MDA-MB-231 cells, respectively; over expression of TRF2 devoid of DNA binding [deletion of basic (delB), myb (delM) & both basic/myb (delB-delM) domains] resulted in partial or complete rescue of p21 promoter activity in HT1080 & MDA-MB-231 cells (data represented as mean ± SEM, for three replicates) (C). (D,E) HT1080 cells over expressing TRF2 show reduced p21 protein expression, bar graph shows the densitometry analysis of three different immunoblot replicates (*p value < 0.05, Student’s t-test; data represented as mean ± SEM of three replicates). (E) (Full images are shown in Supplementary Figure S5); TRF2 silencing results in increase in p21 protein, bar graph shows the densitometry analysis of three different immunoblots (*p value < 0.05, Student’s t-test; data represented as mean ± SEM of three replicates) (F); & mRNA expression in HT1080 cells (*p value < 0.05, Student’s t-test; data represented as mean ± SEM of three replicates, GAPDH used as internal control for real-time PCR). Image collected & cropped by CiteAb from the following publication (//www.nature.com/articles/s41598-017-11177-1), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-57130_rabbit-polyclonal-trf-2-antibody-31020241624927.jpg)
![Western Blot: TRF-2 Antibody - BSA Free [NB110-57130] - Attenuation of bortezomib-induced shelterin protein dysregulation by hTERT over-expressionA. & B. Cells expressing ectopic hTERT were treated with bortezomib for 24 hours & mRNA levels of shelterin proteins then analyzed using qPCR. The levels of each target mRNA in bortezomib-treated cells were expressed as percentages of those in untreated cells. (A) HEL-hTERT cells & (B) BGC-823-hTERT cells. C. & D. Immunoblotting assessment of TRF1, TRF2 & POT1 protein expression in bortezomib-treated cells. Same sets of cells above were analyzed for TRF1, TRF2 & POT1 protein levels & shown was representative of three independent experiments. (C) HEL-hTERT cells & (D) BGC-823-hTERT cells.* & **: P < 0.05 & 0.01, respectively. BTZ, bortezomib. Image collected & cropped by CiteAb from the following publication (//www.oncotarget.com/lookup/doi/10.18632/oncotarget.5752), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-57130_rabbit-polyclonal-trf-2-antibody-310202416235529.jpg)
![Western Blot: ATM Antibody (2C1) [NB100-309] - Detection of human ATM protein using ATM antibody (2C1) [NB100-309] by western blot or immunoprecipitation. Theoretical molecular weight 351 kDa.](http://images.novusbio.com/fullsize/ATM-Antibody-2C1-Western-Blot-NB100-309-img0018.jpg "Western Blot: ATM Antibody (2C1) [NB100-309] - Detection of human ATM protein using ATM antibody (2C1) [NB100-309] by western blot or immunoprecipitation. Theoretical molecular weight 351 kDa.")
![Immunohistochemistry-Paraffin: ATM Antibody (2C1) [NB100-309] - Human breast carcinoma. ATM stained by ATM antibody [2C1] diluted at 1:100.Antigen Retrieval: Citrate buffer, pH 6.0, 15 min.](http://images.novusbio.com/fullsize/ATM-Antibody-2C1-Immunohistochemistry-Paraffin-NB100-309-img0021.jpg)
![Western Blot: ATM Antibody (2C1) [NB100-309] - Analysis of ATM in U2OS sarcoma cells using ATM antibody (2C1) [NB100-309]. Theoretical molecular weight 351 kDa. Western blot image submitted by a verifeid customer review.](http://images.novusbio.com/fullsize/ATM-Antibody-2C1-Western-Blot-NB100-309-img0010.jpg)
![Immunohistochemistry-Paraffin: ATM Antibody (2C1) [NB100-309] - Human Kidney (formalin-fixed, paraffin-embedded) stained with ATM antibody (2C1) [NB100-309] at 5 ug/ml followed by biotinylated anti-mouse IgG secondary antibody, alkaline phosphatase-streptavidin and chromogen.](http://images.novusbio.com/fullsize/ATM-Antibody-2C1-Immunohistochemistry-Paraffin-NB100-309-img0012.jpg)
![<b>Genetic Strategies Validation. </b>Western Blot: ATM Antibody (2C1) [NB100-309] - Non-transfected (-) and transfected (+) HeLa whole cell extracts (60 ug) were separated by 5% SDS-PAGE, and the membrane was blotted with ATM antibody (2C1) [NB100-309] diluted at 1:500.](http://images.novusbio.com/fullsize/ATM-Antibody-2C1-Knockdown-Validated-NB100-309-img0017.jpg)
![<b>Genetic Strategies Validation. </b>Western Blot: ATM Antibody (2C1) [NB100-309] - Methylated EDSBs may be repaired by an ATM-dependent pathway. Immunoblots of ATM and DNA-PKcs in ATM shRNA-transfected HeLa cells, using ATM antibody (2C1) [NB100-309]. GAPDH is included as a loading control. Image collected and cropped by CiteAb from the following publication (//molecular-cancer.biomedcentral.com/articles/10.1186/1476-4598-9-70), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/ATM-Antibody-2C1-Western-Blot-NB100-309-img0019.jpg)
![Immunoprecipitation: ATM Antibody (2C1) [NB100-309] - MDA-MB-231 whole cell lysates were immunoprecipitated with 2 ug ATM Antibody (NB100-309), followed by Western blot (primary antibody: NB100-309 at 1:1000, 4C overnight. Western blot image submitted by a verified customer review.](http://images.novusbio.com/fullsize/ATM-Antibody-2C1-Western-Blot-NB100-309-img0020.jpg)
![<b>Biological Strategies Validation. </b>Western Blot: ATM Antibody (2C1) [NB100-309] - MCELNs decreased the DNA damage of H9C2 cells after radiation. Western blot images of p-ATM (NB100-306) and ATM (NB100-309) in H9C2 cells after 48 h of culture with indicated treatment. IR (-/+): 0/16 Gy X-ray; MCELNs (-/+): 0/10 ug/mL. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/35509278/) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/nb100-309_mouse-monoclonal-atm-antibody-2c1-25520231514910.jpg)
![Western Blot: ATM Antibody (2C1) [NB100-309] - Western blot analysis of the extent of knockdown MRE11 & ATM, & the lack of effect of Mirin activation of ATM. The extent of shRNA-mediated knockdown of MRE11 & ATM are shown for (A) clones GFP-7F1 & GFP-6D1 & (B) clones EDS-7F2 & EDS-6J8. The extent of knockdown was determined by analyzing the intensity of the ATM & MRE11 bands relative to the intensity of the loading control GAPDH bands (see Table 1). (C) The effect of Mirin on activation of ATM was determined by analysis of phosphorylation of ATM in response to ionizing radiation. Cultures treated with DMSO alone, 20 μM Mirin, or knockdown of ATM were analyzed by western blot 30 min after exposure to 10 Gy of ionizing radiation. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/26209132), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-309_mouse-monoclonal-atm-antibody-2c1-310202415371910.jpg)
![Western Blot: ATM Antibody (2C1) [NB100-309] - Rac1 inhibition abolishes IR-induced activation of both ATM & ATR signaling. (A) MCF-7 cells were treated with/without 20-Gy IR in the presence or absence of 100 μM NSC23766 & incubated for 1 hour at 37°C before analysis. To assess the ATM kinase activity, ATM was immunoprecipitated from cell lysate by using anti-ATM antibody (2C1) & assayed for ATM activity by using p53 recombinant protein as substrate. To measure the Chk2 activity, Chk2 was immunoprecipitated from cell lysate by using B-4 anti-Chk2 antibody & assayed for Chk2 activity by using Cdc25C recombinant protein as substrate. As controls, ATM & Chk2 protein levels in the immunoprecipitates (IP-WB) as well as in cell lysates (WB) were assessed with immunoblotting. (B) ATR & Chk1 were immunoprecipitated from cell lysates by using N-19 anti-ATR & G-4 anti-Chk1 antibody, respectively. ATR activity was assayed by using p53 recombinant protein substrate, & Chk1 activity assayed by using Cdc25C recombinant protein substrate. As controls, ATR & Chk1 protein levels in the immunoprecipitates (IP-WB), as well as in cell lysates (WB) were assessed with immunoblotting. (C) MCF-7 cells were exposed to IR at the indicated doses in the presence or absence of NSC23766, incubated for 1 hour, & assessed for Chk1 & Chk2 activities. *Kinase assay does not contain Cdc25C substrate. (D) T47D & ZR-75-1 cells were exposed to 10-Gy IR in the presence or absence of 100 μM NSC23766, incubated for 1 hour, & analyzed for Chk1 & Chk2 activities. Image collected & cropped by CiteAb from the following publication (//breast-cancer-research.biomedcentral.com/articles/10.1186/bcr3164), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-309_mouse-monoclonal-atm-antibody-2c1-310202415535119.jpg)
![Western Blot: ATM Antibody (2C1) [NB100-309] - Inhibition of Rac1 by N17Rac1 mutant or Rac1 siRNA diminishes IR-induced G2/M checkpoint activation. (A) MCF-7 cells were infected with Ad.N17Rac1 or Ad.Control for 24 hours & exposed to 15-Gy IR. Left panel: the cells were analyzed for DNA content 24 hours after IR. The result depicts the percentage of cells with 4N-DNA content & is shown as mean ± SD of quadruplicate samples. *P < 0.001 (n = 4), significant difference from the irradiated Ad.Control-infected cells. Right panel: Inset: at 15 minutes after IR, the infected cells were analyzed for Rac1 activities (Rac1-GTP) & protein levels (total Rac1). Bar graph: mitotic cells in the cell samples were analyzed 2 hours after IR. The result depicts the percentage of mitotic cells & is shown as mean ± SD of triplicate samples. **P = 0.002 (n = 3), significant difference from the irradiated Ad.Control-infected cells. (B) Upper panel: MCF-7 cells transfected with Rac1 siRNA (Rac1) or control siRNA (Control) were incubated for the indicated times & analyzed for protein levels of Rac1 & Actin. Lower panel: After 2-day incubation, the siRNA-transfected cells were exposed to IR, incubated for 24 hours, & assessed for DNA content. Results depict the percentage of cells with 4N-DNA content & represent the mean ± SD of three separate experiments in duplicate samples. *P < 0.001 (n = 6), significant difference from the irradiated Control-siRNA transfected cells. (C) After 2-day incubation, siRNA-transfected cells were treated with/without 20-Gy IR, incubated for 1 hour, & analyzed for ATM, ATR, Chk1, & Chk2 activities. Image collected & cropped by CiteAb from the following publication (//breast-cancer-research.biomedcentral.com/articles/10.1186/bcr3164), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-309_mouse-monoclonal-atm-antibody-2c1-310202415525285.jpg)
![Western Blot: ATM Antibody (2C1) [NB100-309] - HeLa whole cell extract and nuclear extracts (30 ug) were separated by 5% SDS-PAGE, and the membrane was blotted with ATM antibody [2C1] (NB100-309) diluted at 1:500. The HRP-conjugated anti-mouse IgG antibody was used to detect the primary antibody.](http://images.novusbio.com/fullsize/nb100-309_mouse-monoclonal-atm-antibody-2c1-91020242041241.jpg)
![Western Blot: ATM Antibody (2C1) [NB100-309] - Whole cell extract (30 ug) was separated by 5% SDS-PAGE, and the membrane was blotted with ATM antibody [2C1] (NB100-309) diluted at 1:1000.](http://images.novusbio.com/fullsize/nb100-309_mouse-monoclonal-atm-antibody-2c1-91020242063311.jpg)
![Simple Western: TRF-2 Antibody (4A794.15) [NB100-56506] - Image shows a specific band for TRF2 in 1.0 mg/mL of HeLa lysate. This experiment was performed under reducing conditions using the 12-230 kDa separation system. Non-specific interaction with the 230 kDa Simple Western standard may be seen with this antibody.](http://images.novusbio.com/fullsize/TRF-2-Antibody-4A794-15-Simple-Western-NB100-56506-img0010.jpg "Simple Western: TRF-2 Antibody (4A794.15) [NB100-56506] - Image shows a specific band for TRF2 in 1.0 mg/mL of HeLa lysate. This experiment was performed under reducing conditions using the 12-230 kDa separation system. Non-specific interaction with the 230 kDa Simple Western standard may be seen with this antibody.")
![Western Blot: TRF-2 Antibody (4A794.15) [NB100-56506] - Analysis in human Jurkat cell lysate at 2 ug/mL. Goat anti-mouse Ig HRP secondary antibody and PicoTect ECL substrate solution were used.](http://images.novusbio.com/fullsize/TRF-2-Antibody-4A794-15-Western-Blot-NB100-56506-img0008.jpg)
![Immunohistochemistry-Paraffin: TRF-2 Antibody (4A794.15) [NB100-56506] - Transitional cell carcinoma, urinary bladder, stained with TRF2 antibody (4 ug/mL), peroxidase-conjugate and DAB chromogen. Note specific nuclear staining. Tumor/normal adjacent tissue array slide was used for this test. Staining of formalin-fixed tissues is enhanced by boiling tissue sections in 10 mM sodium citrate buffer, pH 6.0 for 10-20 min followed by cooling at RT for 20 min.](http://images.novusbio.com/fullsize/TRF-2-Antibody-4A794-15-Immunohistochemistry-Paraffin-NB100-56506-img0012.jpg)
![Immunocytochemistry/Immunofluorescence: TRF-2 Antibody (4A794.15) [NB100-56506] - Localization of candidate RNAs at telomeres. Localization of SNORD17 at telomeres in human U-2 OS cells. Cells were fixed and sequentially incubated with Abs against TRF-2 and AlexaFluor 488-conjugated anti-mouse IgG. Subsequently, the cells were hybridized with the RNA probes and subjected to fluorescence microscopy. Three different cells are shown. Image collected and cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0123387), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/TRF-2-Antibody-4A794-15-Immunocytochemistry-Immunofluorescence-NB100-56506-img0018.jpg)
![Flow Cytometry: TRF-2 Antibody (4A794.15) [NB100-56506] - Intracellular flow cytometric analysis of TRF2 in 10^6 human Jurkat cells using 0.1 ug of NB100-56506. The shaded histogram represents cells alone, blue represents isotype control and red represents NB100-56506, anti-TRF2.](http://images.novusbio.com/fullsize/TRF-2-Antibody-4A794-15-Flow-Cytometry-NB100-56506-img0001.jpg)
![Western Blot: TRF-2 Antibody (4A794.15) [NB100-56506] - Total protein from mouse 3T3 cells was separated on a 12% gel by SDS-PAGE, transferred to PVDF membrane and blocked in 5% non-fat milk in TBST. The membrane was probed with 2.0 ug/mL anti-TRF2 in 1% non-fat milk in TBST and detected with an anti-mouse HRP secondary antibody using chemiluminescence.](http://images.novusbio.com/fullsize/TRF-2-Antibody-4A794-15-Western-Blot-NB100-56506-img0016.jpg)
![Immunocytochemistry/Immunofluorescence: TRF-2 Antibody (4A794.15) [NB100-56506] - Localization of candidate RNAs at telomeres. Localization of NEAT1 at telomeres in human U-2 OS cells. Cells were fixed and sequentially incubated with Abs against TRF-2 and AlexaFluor 488-conjugated anti-mouse IgG. Subsequently, the cells were hybridized with the RNA probes and subjected to fluorescence microscopy. Three different cells are shown. Image collected and cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0123387), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/TRF-2-Antibody-4A794-15-Immunocytochemistry-Immunofluorescence-NB100-56506-img0019.jpg)
![Flow Cytometry: TRF-2 Antibody (4A794.15) [NB100-56506] - An intracellular stain was performed on A431 cells with TRF2 Antibody [4A794.15] NB100-56506 (blue) and a matched isotype control (orange). Cells were fixed with 4% PFA and then permeabilized with 0.1% saponin. Cells were incubated in an antibody dilution of 1.0 ug/mL for 30 minutes at room temperature, followed by Mouse IgG (H+L) Cross-Adsorbed Secondary Antibody, Dylight 550 (35503, Thermo Fisher).](http://images.novusbio.com/fullsize/TRF-2-Antibody-4A794-15-Flow-Cytometry-NB100-56506-img0020.jpg)
![Immunocytochemistry/Immunofluorescence: TRF-2 Antibody (4A794.15) [NB100-56506] - Staining of TRF2-bound telomeres in human HeLa cells (Courtesy of Fotiadou, et al, 2004).](http://images.novusbio.com/fullsize/TRF-2-Antibody-4A794-15-Immunocytochemistry-Immunofluorescence-NB100-56506-img0005.jpg)
![Immunocytochemistry/Immunofluorescence: TRF-2 Antibody (4A794.15) [NB100-56506] - HeLa cells were fixed for 10 minutes using 10% formalin and then permeabilized for 5 minutes using 1X PBS + 0.5% Triton-X100. The cells were incubated with anti-TRF-2 (4A794.15) conjugated to FITC [NB100-56506F] at 5 ug/mL for 1 hour at room temperature. Nuclei were counterstained with DAPI (Blue). Cells were imaged using a 40X objective.](http://images.novusbio.com/fullsize/TRF-2-Antibody-4A794-15-Immunocytochemistry-Immunofluorescence-NB100-56506-img0017.jpg)
![Immunocytochemistry/ Immunofluorescence: TRF-2 Antibody (4A794.15) - BSA Free [NB100-56506] - ZBTB48‐dependent loss of MTFP1 phenocopies MTFP1 depletionFluorescence microscopy analysis of the structure & localization of the mitochondrial network in HeLa WT & ZBTB48 KO clones. Mitochondria are marked with the MitoTracker dye (red), & nuclei are counterstained with DAPI (blue). Scale bars represent 20 μm.The same analysis as in (A) for U2OS WT & ZBTB48 KO clones. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28500257), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-56506_mouse-monoclonal-trf-2-antibody-4a794-15-31020241534325.jpg)
![Western Blot: TRF-2 Antibody (4A794.15) - BSA Free [NB100-56506] - TRF2 delta B delta M expression induces chromosome end-to-end fusions in all inducible cell lines(A) Immunoblots of MCF-10A, TO, SH-TO & SV-TO cell lines with & without DOX & HEK 293T. After 96 h of DOX treatment, the inducible cell lines expressed the truncated TRF2 delta B delta M protein (50 kDa); in contrast, uninduced cell lines, MCF-10A parental cell line & HEK 293T cells displayed only the endogen TRF2 protein (66 kDa). Lamin B1 was used as loading control. (B) After sustained expression of TRF2 delta B delta M for 96 h there was a significant increase in aberrant metaphases only in TO cells when compared to uninduced matched cells. (C) Nevertheless, the efficacy of the inducible system was validated by the statistical increase of cells with end-to-end fusions in all inducible cell lines. (D) Moreover, a high incidence of fusions per cell was found in all modified cell lines after sustained TRF2 depletion. Data was presented as mean + SEM. (E) Example of TO, SH-TO & SV-TO karyotypes after 96 h of TRF2 delta B delta M expression. Open arrows indicate clonal aberrations in the parental MCF-10A cell line. Insets in the karyotype show rearranged chromosomes stained with centromeric (green) & telomeric (red) PNA probes. Note the presence of telomere FISH signals at the fusion point of chromatid- or chromosome-type end-to-end fusions. Image collected & cropped by CiteAb from the following publication (//www.oncotarget.com/lookup/doi/10.18632/oncotarget.25502), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-56506_mouse-monoclonal-trf-2-antibody-4a794-15-31020241682158.jpg)
![Immunocytochemistry/ Immunofluorescence: TRF-2 Antibody (4A794.15) - BSA Free [NB100-56506] - ZBTB48 ZnF11 necessary to bind to telomeres. Sequence‐specific DNA pull‐downs w/ either telomeric (TTAGGG)/a control sequence (GTGAGT) for FLAG‐ZBTB48 WT, domain deletion constructs for different zinc finger & combinations of deletion constructs w/ ZnF10/11 point mutants. Domain structures indicated - right.Sequence‐specific DNA pull‐downs for FLAG‐ZBTB48 WT & ZnF11 point mutant for telomeric repeat sequences of different phyla (green) & their respective scrambled controls (blue).Protein expression analysis of ZBTB48 by WB for cell lines used. GAPDH serves as a loading control.IF stainings for exogenous FLAG‐ZBTB48 WT & point mutants for ZnF10 & ZnF11 in U2OS cells. The same analysis as in Fig 1E performed & average co‐localization frequencies shown (n = 24–37 cells).Co‐localization analysis of endogenous ZBTB48/exogenous FLAG‐ZBTB48 WT w/ TRF2 in HeLa cells by IF (IF) staining. Image illustrating co‐localization between ZBTB48/FLAG‐ZBTB48 WT (green) & TRF2 (red) as a marker for telomeres is shown w/ DAPI (blue) used as nuclear counterstain. Co‐localization events indicated by white arrows. Quantification of frequency of co‐localization events (right) done after 3D reconstruction of acquired z‐stacks (n = 30 cells).Co‐localization analysis of endogenous ZBTB48/exogenous FLAG‐ZBTB48 WT w/ TRF2 in HeLa 1.3 cells by IF (IF) staining analogous to (E) (n = 30 cells).Co‐localization analysis of endogenous ZBTB48/exogenous FLAG‐ZBTB48 WT w/ TRF2 in HT1080 super‐telomerase cells by IF (IF) staining analogous to (E) (n = 30 cells).Data information: (D–G) Scale bars = 5 μm. Error bars indicate standard deviations, & P‐values based on Student's t‐test.Source data available online for this figure. Image collected & cropped by CiteAb from following publication (//pubmed.ncbi.nlm.nih.gov/28500257), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-56506_mouse-monoclonal-trf-2-antibody-4a794-15-31020241553721.jpg)
![Western Blot: ATM Antibody [NB100-104] - Detection of ATM in HeLa nuclear extract using ATM antibody [NB100-104]. Theoretical molecular weight 351 kDa.](http://images.novusbio.com/fullsize/ATM-Antibody-Western-Blot-NB100-104-img0009.jpg "Western Blot: ATM Antibody [NB100-104] - Detection of ATM in HeLa nuclear extract using ATM antibody [NB100-104]. Theoretical molecular weight 351 kDa.")
![Immunohistochemistry-Paraffin: ATM Antibody [NB100-104] - Staining of human tonsil, germinal center and mantle zone with ATM Antibody [NB100-104].](http://images.novusbio.com/fullsize/ATM-Antibody-Immunohistochemistry-Paraffin-NB100-104-img0014.jpg)
![<b>Biological Strategies Validation. </b>Immunocytochemistry/Immunofluorescence: ATM Antibody [NB100-104] - GM00637 cells with KU55933 pretreatment (a) were exposed to 50 uM spermidine or CCCP, followed by immunofluorescence analyses of total and p-ATM on Ser-1981. The scale bar is 10 um. Image collected and cropped by CiteAb from the following publication (//www.nature.com/articles/srep24700) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/ATM-Antibody-Immunocytochemistry-Immunofluorescence-NB100-104-img0018.jpg)
![Flow Cytometry: ATM Antibody [NB100-104] - An intracellular stain was performed on HeLa cells with Dylight 550-conjugated ATM Antibody [NB100-104R] (blue) and a matched isotype control (orange). Cells were fixed with 4% PFA and then permeabilized with 0.1% saponin. Cells were incubated in an antibody dilution of 5 ug/mL for 30 minutes at room temperature. Both antibodies were conjugated to DyLight 550.](http://images.novusbio.com/fullsize/ATM-Antibody-Flow-Cytometry-NB100-104-img0016.jpg)
![<b>Biological Strategies Validation. </b>Western Blot: ATM Antibody [NB100-104] - Analysis of double strand break repair in MCF-7 monolayer and mammosphere populations. Expression of proteins involved in the NHEJ pathway of DSB repair in response to increasing doses of ionizing radiation. Lysates were prepared from unirradiated cells and from cells harvested one hour after exposure to 1 or 10-Gy 60Co I3-radiation and analyzed by immunoblotting with antibodies against several DSB repair proteins. Phospho-ATM and phospho-DNA-PKcs refer to phosphorylation of these proteins at Ser1981 and Ser2056, respectively. Actin served as a loading control. Image collected and cropped by Citeab from the following publication (Senescence evasion by MCF-7 human breast tumor-initiating cells. Breast Cancer Res (2010)) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/ATM-Antibody-Western-Blot-NB100-104-img0017.jpg)
![Western Blot: ATM Antibody [NB100-104] - Detection of ATM in Raji whole cell lysate using [NB100-104]. Observed molecular weight ~300 kDa. Theoretical molecular weight 351 kDa.](http://images.novusbio.com/fullsize/ATM-Antibody-Western-Blot-NB100-104-img0001.jpg)
![Immunocytochemistry/Immunofluorescence: ATM Antibody [NB100-104] - HeLa cells were fixed for 10 minutes using 10% formalin and then permeabilized for 5 minutes using 1X TBS + 0.05% Triton X-100. Then cells were incubated with [NB100-104] at a 1:100 dilution overnight at 4C and detected with an anti-rabbit DyLight 488 (Green) at a 1:500 dilution. Alpha tubulin was used as a co-stain at a 1:1000 dilution and detected with an anti-mouse DyLight 550 (Red) at a 1:500 dilution. Nuclei were counterstained with DAPI (Blue). Cells were imaged using a 40X objective.](http://images.novusbio.com/fullsize/ATM-Antibody-Immunocytochemistry-Immunofluorescence-NB100-104-img0011.jpg)
![Flow Cytometry: ATM Antibody [NB100-104] - Analysis of PE conjugate of ATM Antibody [NB100-104PE]. An intracellular stain was performed on HeLa cells with ATM antibody [NB100-104PE] (blue) and a matched isotype control [NBP2-24893PE] (orange). Cells were fixed with 4% PFA and then permeablized with 0.1% saponin.](http://images.novusbio.com/fullsize/ATM-Antibody-Flow-Cytometry-NB100-104-img0012.jpg)
![Flow Cytometry: ATM Antibody [NB100-104] - An intracellular stain was performed on HepG2 cells with PE-conjugated ATM antibody [NB100-104PE] (blue) and a matched isotype control (orange). Cells were fixed with 4% PFA and then permeablized with 0.1% saponin. Cells were incubated in an antibody dilution of 5 ug/mL for 30 minutes at room temperature. Both antibodies were conjugated to Phycoerythrin.](http://images.novusbio.com/fullsize/ATM-Antibody-Flow-Cytometry-NB100-104-img0015.jpg)
![Immunocytochemistry/ Immunofluorescence: ATM Antibody [NB100-104] - ATM is activated by spermidine in GM00637 cells.GM00637 cells with or without KU55933 pretreatment (a,b), & GM05849 cells (c) were exposed to 50 μM spermidine or CCCP, followed by immunofluorescence analyses of total & p-ATM on Ser-1981. The scale bar is 10 μm. Ratios of cells expressing p-ATM Ser-1981 to cells expressing total ATM were presented (d). 20–45 cells/condition from three experiments were collected. Values are mean ± SD, *p < 0.05 vs. control. Image collected & cropped by CiteAb from the following publication (//www.nature.com/articles/srep24700), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-104_rabbit-polyclonal-atm-antibody-31020241535641.jpg)
![Immunocytochemistry/ Immunofluorescence: ATM Antibody [NB100-104] - ATM is activated by spermidine in GM00637 cells.GM00637 cells with or without KU55933 pretreatment (a,b), & GM05849 cells (c) were exposed to 50 μM spermidine or CCCP, followed by immunofluorescence analyses of total & p-ATM on Ser-1981. The scale bar is 10 μm. Ratios of cells expressing p-ATM Ser-1981 to cells expressing total ATM were presented (d). 20–45 cells/condition from three experiments were collected. Values are mean ± SD, *p < 0.05 vs. control. Image collected & cropped by CiteAb from the following publication (//www.nature.com/articles/srep24700), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-104_rabbit-polyclonal-atm-antibody-310202415304298.jpg)
![Western Blot: ATM Antibody [NB100-104] - Depletion of SMARCAL1 induces DNA damage & checkpoint activation in iSML1 iPSCs. (A,B) The iSML1 iPSCs were cultured for 7 & 14 days in the presence of doxycycline (DOX) to induce SMARCAL1 downregulation & then immunostained. The graphs (top) show quantification of the number of gamma -H2AX-positive cells (A) or ATM-pSer1981-positive cells (B). Representative images from triplicate experiments are shown (bottom). (C) Immunoblot detection of the indicated DDR proteins in iSML1 iPSCs after 14 days of continuous treatment with DOX. Lamin B1 was used as the loading control. Data are mean±s.e.m. from three independent experiments. *P≤0.05, **P≤0.01, ***P≤0.001 (two-way ANOVA test). ns, not significant. Scale bars: 10 µm. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31515241), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-104_rabbit-polyclonal-atm-antibody-310202415371997.jpg)
![Western Blot: ATM Antibody [NB100-104] - Analysis of double strand break repair in MCF-7 monolayer & mammosphere populations. (a) Cells were exposed to 4 Gy 60Co gamma -radiation & the relative degree of double-strand breakage (DSB) was determined by the comet assay under neutral conditions immediately after exposure & at the times indicated after exposure. (b) The 'comets' (n of about 100) were categorized according to the NIH LISTSERV (Comet Assay Interest Group web site) in which type 1 comets display the least DNA damage & type 5 the most. The error bars represent the mean ± standard error of the mean in both panels. The comets of the unirradiated cells are labeled Cont. (c) Expression of proteins involved in the NHEJ pathway of DSB repair in response to increasing doses of ionizing radiation. Lysates were prepared from unirradiated cells & from cells harvested one hour after exposure to 1 or 10-Gy 60Co gamma -radiation & analyzed by immunoblotting with antibodies against several DSB repair proteins. Phospho-ATM & phospho-DNA-PKcs refer to phosphorylation of these proteins at Ser1981 & Ser2056, respectively. Actin served as a loading control. Image collected & cropped by CiteAb from the following publication (//breast-cancer-research.biomedcentral.com/articles/10.1186/bcr2583), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-104_rabbit-polyclonal-atm-antibody-310202415535196.jpg)
![Simple Western: Rad50 Antibody [NB100-154] - Simple Western lane view shows a specific band for Rad50 in 0.5 mg/ml of HeLa lysate. This experiment was performed under reducing conditions using the 12-230 kDa separation system.](http://images.novusbio.com/fullsize/Rad50-Antibody-Simple-Western-NB100-154-img0004.jpg "Simple Western: Rad50 Antibody [NB100-154] - Simple Western lane view shows a specific band for Rad50 in 0.5 mg/ml of HeLa lysate. This experiment was performed under reducing conditions using the 12-230 kDa separation system.")
![Western Blot: Rad50 Antibody [NB100-154] - Mre11-deficient ATLD1 cells are resistant to MK-8776. Whole cell lysates from U2OS, ATLD1 and ATLD1+Mre11 cells were analyzed by western blot for proteins of the MRN complex. Image collected and cropped by CiteAb from the following publication (//doi.org/10.1371/journal.pone.0044021) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/Rad50-Antibody-Western-Blot-NB100-154-img0006.jpg)
![Western Blot: Rad50 Antibody [NB100-154] - WB detection of RAD50 protein in 30ug whole cell lysate of 293T cells using Rad50 antibody at 1:2000 dilution (Submitted via Verified Customer Review).](http://images.novusbio.com/fullsize/Rad50-Antibody-Western-Blot-NB100-154-img0005.jpg)
![Western Blot: Rad50 Antibody [NB100-154] - Detection of Rad50 in HeLa nuclear extracts.](http://images.novusbio.com/fullsize/Rad50-Antibody-Western-Blot-NB100-154-img0002.jpg)
![Western Blot: ATM Antibody (5C2) [NB100-220] - HeLa whole cell and nuclear extracts (30 ug) were separated by 5% SDS-PAGE, and the membrane was blotted with ATM antibody (5C2) [NB100-220] diluted at 1:1000. The HRP-conjugated anti-mouse IgG antibody [NBP2-19382] was used to detect the primary antibody, and the signal was developed with Trident ECL plus-Enhanced. Observed molecular weight ~320 kDa. Theoretical molecular weight 351 kDa.](http://images.novusbio.com/fullsize/ATM-Antibody-5C2-Western-Blot-NB100-220-img0007.jpg "Western Blot: ATM Antibody (5C2) [NB100-220] - HeLa whole cell and nuclear extracts (30 ug) were separated by 5% SDS-PAGE, and the membrane was blotted with ATM antibody (5C2) [NB100-220] diluted at 1:1000. The HRP-conjugated anti-mouse IgG antibody [NBP2-19382] was used to detect the primary antibody, and the signal was developed with Trident ECL plus-Enhanced. Observed molecular weight ~320 kDa. Theoretical molecular weight 351 kDa.")
![Immunocytochemistry/Immunofluorescence: ATM Antibody (5C2) [NB100-220] - HeLa cells were fixed in 4% paraformaldehyde at RT for 15 min. Green: ATM protein stained by ATM antibody (5C2) [NB100-220] diluted at 1:200. Blue: Hoechst 33342 staining. Scale bar = 10 um.](http://images.novusbio.com/fullsize/ATM-Antibody-5C2-Immunocytochemistry-Immunofluorescence-NB100-220-img0004.jpg)
![Western Blot: ATM Antibody (5C2) [NB100-220] - Absence of Atm does not relieve the selective pressure to inactivate p53 during chemical carcinogenesis. Examples of cancer cell lines established from 3MC-fibrosarcomas (each line derives from an independent fibrosarcoma). The genotype of the mice where the 3MC-fibrosarcomas were generated is indicated, as well as, the status of p53 as determined by a nutlin-sensitivity assay (see Supplementary Figures S5 and S6). Cell lines were exposed to 10 Gy and protein extracts were obtained 1h and 24h after irradiation. The levels of the indicated proteins were determined by immunoblotting using beta-actin as loading control. Image collected and cropped by CiteAb from the following publication (www.dx.plos.org/10.1371/journal.pone.0005475) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/ATM-Antibody-5C2-Western-Blot-NB100-220-img0008.jpg)
![Western Blot: ATM Antibody (5C2) [NB100-220] - Absence of Atm does not relieve the selective pressure to inactivate p53 during chemical carcinogenesis.A. Representative images of 3MC-fibrosarcomas immunostained for Arf, p53 & p21 (see also Table 1). The upper & middle rows are representative of the large majority of fibrosarcomas developed in wild-type (upper) & Atm-null (middle) mice, which are consistent with a mutant p53 (i.e. strongly positive for p53 & negative for p21). The lower row is representative of the fibrosarcomas developed in Arf-null mice, which are consistent with a functional p53 (i.e. very weakly positive for p53 & positive for p21). B. Examples of cancer cell lines established from 3MC-fibrosarcomas (each line derives from an independent fibrosarcoma). The genotype of the mice where the 3MC-fibrosarcomas were generated is indicated, as well as, the status of p53 as determined by a nutlin-sensitivity assay (see Supplementary Figures S5 & S6). Cell lines were exposed to 10 Gy & protein extracts were obtained 1h & 24h after irradiation. The levels of the indicated proteins were determined by immunoblotting using beta -actin as loading control. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/19421407), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-220_mouse-monoclonal-atm-antibody-5c2-31020241612655.jpg)
![Immunohistochemistry: ATM Antibody (5C2) [NB100-220] - Limited role of Atm in p53-mediated tumor suppression & DNA damage response in chemically-induced fibrosarcomas.A. Mice of the indicated genotypes, wt (n = 15), p53-super (n = 16), Atm-null (n = 9), p53-super/Atm-null (n = 13) & Arf-null (n = 12), were injected intramuscularly with 3-methyl-cholanthrene (3MC) & tumour development was monitored. Kaplan-Meier tumour-free curves were obtained & statistical significant differences (logrank test) were found for wt vs. p53-super (p<0.005), Atm-null vs. p53-super/Atm-null (p<0.001) & Arf-null vs. wt (p<0.0001). No significant differences were found for wt vs. Atm-null (p = 0.11), or p53-super vs. p53-super/Atm-null (p = 0.18). B. Quantification of the persistent DNA damage response ( gamma H2AX), proliferation (Ki67), & apoptosis (activated caspase-3) in 3MC-fibrosarcomas generated in mice of the indicated genotypes. Quantifications are relative to the 3MC-fibrosarcomas in wild-type mice. Values correspond to the average & standard deviation (n = 5 per genotype). Examples of the immunostainings are shown in the panels at the right. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/19421407), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-220_mouse-monoclonal-atm-antibody-5c2-3102024165717.jpg)
![Immunocytochemistry/ Immunofluorescence: ATM Antibody (5C2) [NB100-220] - BAG3P209L aggregation leads to co-aggregation of proteasomal substrates. a Immunofluorescence pictures of HeLa cells expressing FLAG-BAG3WT or FLAG-BAG3P209L using antibodies against BAG3 (green) or ubiquitin (red). Scale bar = 5 μm. b Suppression of GFP-HttQ74 aggregation of cells expressing a control, FLAG-BAG3WT or FLAG-BAG3P209L. Western blot against indicated antibodies is shown. c Quantification of GFP-HttQ74 aggregation of experiments similar to b. Relative percentage of SDS-insoluble protein levels are shown. Data represents the mean & standard deviation of three independent experiments. d Immunofluorescence pictures of HeLa cells expressing FLAG-BAG3WT or FLAG-BAG3P209L using antibodies against BAG3 (green) or ubiquitin (red). Left column BAG3, middle column ubiquitin & right column is the merge of BAG3 (green), ubiquitin (red), & DAPI (blue). Scale bar = 5 μm. e Fractionation of HEK293 cells expressing HSPB8, a control or BAG3WT or BAG3P209L, together with either Ub-R-GFP or GFP-ODC (ornithine decarboxylase). Western blot against GFP, FLAG (BAG3), Myc (HSPB8), & tubulin are shown. f Fractionation of HEK293 cells expressing HSPB8 & indicated BAG3 variants. Western blot using ubiquitin (FK2) & tubulin antibodies are shown. The same samples as in Fig. 5e have been used, loading control is therefore the same. Source data are provided as a Source data file Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30559338), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-220_mouse-monoclonal-atm-antibody-5c2-31020241553206.jpg)
![Immunohistochemistry: ATM [p Ser1981] Antibody (10H11.E12) [NB100-306] - ATM [p Ser1981] antibody (10H11.E12) [NB100-306] was tested in mouse spleen using DAB with hematoxylin counterstain.](http://images.novusbio.com/fullsize/ATM-p-Ser1981-Antibody-10H11-E12-Immunohistochemistry-NB100-306-img0005.jpg "Immunohistochemistry: ATM [p Ser1981] Antibody (10H11.E12) [NB100-306] - ATM [p Ser1981] antibody (10H11.E12) [NB100-306] was tested in mouse spleen using DAB with hematoxylin counterstain.")
![Western Blot: ATM [p Ser1981] Antibody (10H11.E12) [NB100-306] - Analysis of ATM-kinase, using ATM [p Ser1981] antibody (10H11.E12) [NB100-306]. Sample: Irradiated or peroxidated human fibroblasts. Observed molecular weight 370 kDa. Theoretical molecular weight 351 kDa.](http://images.novusbio.com/fullsize/ATM-p-Ser1981-Antibody-10H11-E12-Western-Blot-NB100-306-img0004.jpg)
![Immunocytochemistry/Immunofluorescence: ATM [p Ser1981] Antibody (10H11.E12) [NB100-306] - Human lymphoblastoid cells stained with ATM [p Ser1981] Antibody (10H11.E12). ICC/IF image submitted by a verified customer review.](http://images.novusbio.com/fullsize/ATM-p-Ser1981-Antibody-10H11-E12-Immunocytochemistry-Immunofluorescence-NB100-306-img0006.jpg)
![<b>Biological Strategies Validation. </b>Western Blot: ATM [p Ser1981] Antibody (10H11.E12) [NB100-306] - MCELNs decreased the DNA damage of H9C2 cells after radiation. Western blot images of p-ATM (NB100-306) and ATM (NB100-309) in H9C2 cells after 48 h of culture with indicated treatment. IR (-/+): 0/16 Gy X-ray; MCELNs (-/+): 0/10 ug/mL. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/35509278/) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/nb100-306_mouse-monoclonal-atm-p-ser1981-antibody-10h11-e12-2552023151493.jpg)
![Immunocytochemistry/Immunofluorescence: Mre11 Antibody (12D7) [NB100-473] - Human primary cells stained with Mre11 antibody at a dilution of 1:60. cells were fixed in 1:1 Acetone/Methanol. ICC/IF image submitted by a verified customer review.](http://images.novusbio.com/fullsize/Mre11-Antibody-12D7-Immunohistochemistry-NB100-473-img0008.jpg "Immunocytochemistry/Immunofluorescence: Mre11 Antibody (12D7) [NB100-473] - Human primary cells stained with Mre11 antibody at a dilution of 1:60. cells were fixed in 1:1 Acetone/Methanol. ICC/IF image submitted by a verified customer review.")
![<b>Genetic Strategies Validation. </b>Western Blot: Mre11 Antibody (12D7) [NB100-473] - Non-transfected (-) and transfected (+) HeLa whole cell extracts (30 ug) were separated by 7.5% SDS-PAGE, and the membrane was blotted with Mre11 antibody [12D7] diluted at 1:500. HRP-conjugated anti-mouse IgG antibody (NBP2-19382) was used to detect the primary antibody. A band appears at the theoretical molecular weight of 80 kDa.](http://images.novusbio.com/fullsize/Mre11-Antibody-12D7-Western-Blot-NB100-473-img0010.jpg)
![Western Blot: Mre11 Antibody (12D7) [NB100-473] - Mre11 antibody [12D7] detects Mre11 protein by western blot analysis. A. 30 ug 293T whole cell extract. B. 30 ug whole cell extract of human Mre11-transfected 293T cells. 7.5% SDS-PAGE. Mre11 antibody [12D7] (NB100-473). HRP-conjugated anti-mouse IgG antibody was used to detect the primary antibody. Bands are prominent at the theoretical molecular weight of 80 kDa.](http://images.novusbio.com/fullsize/Mre11-Antibody-12D7-Western-Blot-NB100-473-img0017.jpg)
![Immunocytochemistry/Immunofluorescence: Mre11 Antibody (12D7) [NB100-473] - Analysis of Mre11 antibody (12D7) on lymphoblastoid cells. Dilution 1:200. Image from verified customer review.](http://images.novusbio.com/fullsize/Mre11-Antibody-12D7-Immunocytochemistry-Immunofluorescence-NB100-473-img0021.jpg)
![Immunocytochemistry/Immunofluorescence: Mre11 Antibody (12D7) [NB100-473] - Mre11 antibody [12D7] detects Mre11 protein at nucleus by immunofluorescent analysis. Sample: HeLa cells were fixed in 4% paraformaldehyde at RT for 15 min.Green: Mre11 stained by Mre11 antibody [12D7] (NB100-473).Blue: Hoechst 33342 staining.Scale bar= 10 um.](http://images.novusbio.com/fullsize/Mre11-Antibody-12D7-Immunocytochemistry-Immunofluorescence-NB100-473-img0015.jpg)
![Immunocytochemistry/Immunofluorescence: Mre11 Antibody (12D7) [NB100-473] - Mouse fibroblasts stained with Mre11 Antibody (12D7). ICC/IF image submitted by a verified customer review.](http://images.novusbio.com/fullsize/Mre11-Antibody-12D7-Immunocytochemistry-Immunofluorescence-NB100-473-img0020.jpg)
![Western Blot: Mre11 Antibody (12D7) [NB100-473] - Various whole cell extracts (30 ug) were separated by 7.5% SDS-PAGE, and the membrane was blotted with Mre11 antibody [12D7] (NB100-473) diluted at 1:500. The HRP-conjugated anti-mouset IgG antibody was used to detect the primary antibody.](http://images.novusbio.com/fullsize/nb100-473_mouse-monoclonal-mre11-antibody-12d7-91020242091437.jpg)
![Immunocytochemistry/Immunofluorescence: CEP164 Antibody [NBP1-81445] - Fetuin-A inhibits ciliogenesis. Primary cilia were examined in the absence (CTL) or presence of fetuin-A (FA) by immunostaining with antibodies against acetylated tubulin (Ace-tub), Cep164, IFT88, or Arl13b. Image collected and cropped by CiteAb from the following publication (//www.mdpi.com/1422-0067/20/20/5207), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/CEP164-Antibody-Immunocytochemistry-Immunofluorescence-NBP1-81445-img0014.jpg "Immunocytochemistry/Immunofluorescence: CEP164 Antibody [NBP1-81445] - Fetuin-A inhibits ciliogenesis. Primary cilia were examined in the absence (CTL) or presence of fetuin-A (FA) by immunostaining with antibodies against acetylated tubulin (Ace-tub), Cep164, IFT88, or Arl13b. Image collected and cropped by CiteAb from the following publication (//www.mdpi.com/1422-0067/20/20/5207), licensed under a CC-BY license.")
![Immunohistochemistry-Paraffin: CEP164 Antibody [NBP1-81445] - Staining of human fallopian tube shows strong positivity in cilia in glandular cells.](http://images.novusbio.com/fullsize/CEP164-Antibody-Immunohistochemistry-Paraffin-NBP1-81445-img0012.jpg)
![Immunocytochemistry/Immunofluorescence: CEP164 Antibody [NBP1-81445] - Staining of human cell line U-2 OS shows localization to centrosome. Antibody staining is shown in green.](http://images.novusbio.com/fullsize/CEP164-Antibody-Immunocytochemistry-Immunofluorescence-NBP1-81445-img0007.jpg)
![Immunocytochemistry/Immunofluorescence: CEP164 Antibody [NBP1-81445] - CEP295 overexpression induces extra-long microtubule-based filaments with low efficiency. Schematics on right of D indicate centrioles (black rectangles) and positions of CEP164 (red squares). MC, mother centriole; DC, daughter centriole. Image collected and cropped by CiteAb from the following publication (//jcs.biologists.org/lookup/doi/10.1242/jcs.186338), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/CEP164-Antibody-Immunocytochemistry-Immunofluorescence-NBP1-81445-img0013.jpg)
![Immunohistochemistry-Paraffin: CEP164 Antibody [NBP1-81445] - Staining of human skeletal muscle shows no positivity in myocytes as expected.](http://images.novusbio.com/fullsize/CEP164-Antibody-Immunohistochemistry-Paraffin-NBP1-81445-img0008.jpg)
![Immunohistochemistry-Paraffin: CEP164 Antibody [NBP1-81445] - Staining of human bronchus shows moderate to strong positivity in cilia in respiratory epithelial cells.](http://images.novusbio.com/fullsize/CEP164-Antibody-Immunohistochemistry-Paraffin-NBP1-81445-img0009.jpg)
![Immunohistochemistry-Paraffin: CEP164 Antibody [NBP1-81445] - Staining of human nasopharynx shows strong positivity in cilia in respiratory epithelial cells.](http://images.novusbio.com/fullsize/CEP164-Antibody-Immunohistochemistry-Paraffin-NBP1-81445-img0010.jpg)
![Immunohistochemistry-Paraffin: CEP164 Antibody [NBP1-81445] - Staining of human endometrium shows strong positivity in cilia in glandular cells.](http://images.novusbio.com/fullsize/CEP164-Antibody-Immunohistochemistry-Paraffin-NBP1-81445-img0011.jpg)
![Immunocytochemistry/ Immunofluorescence: CEP164 Antibody [NBP1-81445] - Super-resolution (3D-SIM) microscopic analysis of centriolar distal-end proteins. (a) RPE1 cells were synchronized at G2 phase & immunostained with the indicated antibodies. Lower panels show fluorescence profile plots. Representative images of more than ten cells are presented in (a). ND: nascent daughter centriole, M: mother centriole. (b) The diameters of C2CD3, Talpid3, CEP120, & CEP164 protein spots (n = 30/each). Cumulative data from three independent experiments are shown. ***P < 0.001. (c,d) 3D-SIM analysis of the spatial localizations of C2CD3 (c), Talpid3 (d) & CEP120 (c,d) at the distal ends of centrioles. RPE1 cells were synchronized at G2 phase & immunostained with the indicated antibodies. Scale bar, 100 nm in (a,c,d). (e) Schematic illustration of the spatial localizations of C2CD3, Talpid3, CEP120, & CP110 at the distal ends of centrioles. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30988386), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nbp1-81445_rabbit-polyclonal-cep164-antibody-310202416113546.jpg)
![Immunocytochemistry/ Immunofluorescence: CEP164 Antibody [NBP1-81445] - Depletion of RTTN produces shorter centrioles. a, b U2OS cells were treated with siControl or siRTTN as shown in a, & analyzed by confocal fluorescence microscopy using the indicated antibodies. cHistogram illustrating the distance between the CEP162-positive dots associated with a given pair of orthogonally oriented centrioles. Error bars represent the mean ± s.d.; ***P < 0.001 (two-tailed t-test). d, f PLK4-myc doxycycline (Dox) inducible cells were treated with siControl or siRTTN as shown in a, & then analyzed by confocal fluorescence microscopy using the indicated antibodies d, or by electron microscopy f. e, gHistogram illustrating the length of procentrioles in PLK4-myc-inducible cells, as analyzed by confocal microscopy e or electron microscopy g. Error bars represent the mean ± s.d.; ***P < 0.001 (two-tailed t-test). The procentriole length in b/c was measured as the distance between two CEP162 dots as described by Azimzadeh et al.17 The procentriole length in d/e was measured as the distance between the fluorescent peak intensity of SAS-6 (red) & CEP162 (green) in siControl & siRTTN-treated cells. Scale bar, 5 μm in b & d; Scale bar, 200 nm in f Image collected & cropped by CiteAb from the following publication (//www.nature.com/articles/s41467-017-00305-0), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nbp1-81445_rabbit-polyclonal-cep164-antibody-310202416121961.jpg)
![Immunocytochemistry/ Immunofluorescence: CEP164 Antibody [NBP1-81445] - CPAP-E1235V mutation impaired the recruitment of centriole elongation proteins onto the centrioles. Cells were synchronized in the early S phase by treatment with aphidicolin (2 μg/ml) for 24 h. They were then fixed immediately with methanol (S phase centrioles) or released into fresh culture medium without aphidicolin for another 16 h (G2 phase centrioles). CPAP-WT or mutant cells in the S phase or G2 phase were immunostained with antibodies against the following centriolar proteins. (A) STIL, n = 42 for CPAP-WT; n = 25 for CPAP-E1235V#1; n = 34 for CPAP-E1235V#2. (B) CEP120, n = 50 for CPAP-WT; n = 42 for CPAP-E1235V#1; n = 48 for CPAP-E1235V#2. (C) CENTROBIN, n = 40 for all groups. (D) CEP295, n = 40 for all groups. (E) POC5, n = 42 for CPAP-WT; n = 40 for CPAP-E1235V#1; n = 40 for CPAP-E1235V#2. (F) POC1B, n = 40 for all groups. (G) CEP164, n = 88 for CPAP-WT; n = 74 for CPAP-E1235V#1; n = 38 for CPAP-E1235V#2. All data are presented as mean ±SEM from a pool of n cells from three independent experiments. n.s: not significant; **p < 0.01; ***p < 0.001. Scale bar: 5 μm. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/35309908), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nbp1-81445_rabbit-polyclonal-cep164-antibody-31020241613623.jpg)
![Immunocytochemistry/ Immunofluorescence: CEP164 Antibody [NBP1-81445] - Depletion of RTTN produces shorter centrioles. a, b U2OS cells were treated with siControl or siRTTN as shown in a, & analyzed by confocal fluorescence microscopy using the indicated antibodies. cHistogram illustrating the distance between the CEP162-positive dots associated with a given pair of orthogonally oriented centrioles. Error bars represent the mean ± s.d.; ***P < 0.001 (two-tailed t-test). d, f PLK4-myc doxycycline (Dox) inducible cells were treated with siControl or siRTTN as shown in a, & then analyzed by confocal fluorescence microscopy using the indicated antibodies d, or by electron microscopy f. e, gHistogram illustrating the length of procentrioles in PLK4-myc-inducible cells, as analyzed by confocal microscopy e or electron microscopy g. Error bars represent the mean ± s.d.; ***P < 0.001 (two-tailed t-test). The procentriole length in b/c was measured as the distance between two CEP162 dots as described by Azimzadeh et al.17 The procentriole length in d/e was measured as the distance between the fluorescent peak intensity of SAS-6 (red) & CEP162 (green) in siControl & siRTTN-treated cells. Scale bar, 5 μm in b & d; Scale bar, 200 nm in f Image collected & cropped by CiteAb from the following publication (//www.nature.com/articles/s41467-017-00305-0), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nbp1-81445_rabbit-polyclonal-cep164-antibody-310202416114711.jpg)
![Immunoprecipitation: TRF-2 Antibody [NB100-56694] - Analysis of TRF-2 in HL60 cells. Lane 1. IP (mouse anti-TRF2). Lane 2. IP with control mouse IgG. Lane 3 IP with goat anti-TRF2. Lane 4. IP with pre-immune goat Ig. Lanes 1-4. WB. TRF2 is detected as a ~ 66 kD protein.](http://images.novusbio.com/fullsize/TRF-2-Antibody-Immunoprecipitation-NB100-56694-img0006.jpg "Immunoprecipitation: TRF-2 Antibody [NB100-56694] - Analysis of TRF-2 in HL60 cells. Lane 1. IP (mouse anti-TRF2). Lane 2. IP with control mouse IgG. Lane 3 IP with goat anti-TRF2. Lane 4. IP with pre-immune goat Ig. Lanes 1-4. WB. TRF2 is detected as a ~ 66 kD protein.")
![Immunohistochemistry-Paraffin: TRF-2 Antibody [NB100-56694] - Analysis of Human Tonsil using TRF-2 antibody.](http://images.novusbio.com/fullsize/TRF-2-Antibody-Immunohistochemistry-Paraffin-NB100-56694-img0005.jpg)
![<b>Genetic Strategies Validation. </b>Western Blot: TRF-2 Antibody [NB100-56694] - U2OS cells were transduced with a lentiviral vector coding for a Dox inducible control shRNA (shCtrl) or a shRNA against TRF-2 (shTRF2) and selected with puromycin +/- Dox for a week. A) Western blot analysis of TRF-2 expression one week post selection. Membranes were also probed with anti-tubulin antibodies to show the input material loaded. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32320442/) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/TRF-2-Antibody-Knockdown-Validated-NB100-56694-img0007.jpg)
![<b>Genetic Strategies Validation. </b>Immunocytochemistry/ Immunofluorescence: TRF-2 Antibody [NB100-56694] - U2OS cells were transduced with a lentiviral vector coding for a Dox inducible control shRNA (shCtrl) or a shRNA against TRF-2 (shTRF2) and selected with puromycin +/- Dox for a week. One week post selection, +Dox cells were infected with HHV-6A for 48h and processed for IFA using anti-TRF-2 (green) and anti-IE2 (red). Cells with IE2 in punctate form and cells with large patchy IE2, likely to represent VRC, are shown. Nuclei are outlined by dashed lines. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32320442/) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/TRF-2-Antibody-Knockdown-Validated-NB100-56694-img0008.jpg)
![Western Blot: TRF-2 Antibody [NB100-56694] - TRF2 knockdown affect HHV-6A/B chromosomal integration.A) U2OS cells were transduced with lentiviral vectors expressing a scrambles shRNA (shCtrl) or a shTRF2. After a week of selection, cells were monitored for TRF2 expression by western blot. B) After a week of selection, shCtrl & shTRF2 treated cells were infected with HHV-6A or HHV-6B. After 30 days, DNA was isolated & the relative frequency of integration, relative to shCtrl set at 100%, estimated by ddPCR. *p<0.05. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32320442), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-56694_goat-polyclonal-trf-2-antibody-310202415345328.jpg)
![Immunocytochemistry/ Immunofluorescence: TRF-2 Antibody [NB100-56694] - TRF2 expression in HHV-6A-infected U2OS cells.U2OS cells were infected with HHV-6A & analyzed for TRF2 & IE2 expression at 24h, 48h & 72h post-infection by dual color immunofluorescence. A) Representative immunofluorescence of TRF2 & IE2 expression in bystander & IE2 expressing cells at 24, 48h & 72h post infection. B) Mean relative TRF2 expression ± SD in uninfected (blue), IE2- (green-uninfected bystander) or IE2+ (red-infected) cells at 24h, 48h & 72h post infection. Each symbol represents the relative TRF2 expression from a single nucleus. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32320442), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-56694_goat-polyclonal-trf-2-antibody-310202415304273.jpg)
![Immunocytochemistry/ Immunofluorescence: TRF-2 Antibody [NB100-56694] - Binding of TRF2 to viral DNA during HHV-6A/B infection.A) Schematic representation of the HHV-6A/B genome. The DR6 probe used for hybridization is shown in red. Uninfected & HHV-6A-infected HSB-2 cells (B-D) or uninfected & HHV-6B-infectd Molt-3 cells (E-F) were analyzed for TRF2 binding to viral DNA using ChIP. The input was hybridized with Alu probe to assess quantity of starting material. Anti-IgG (negative control), anti-PolII (positive control) or TRF2 antibodies were used for immunoprecipitation. B) QPCR detection of GAPDH DNA following ChIP. Results are expressed as fold increase over control IgG. C & E) Eluted DNA was hybridized with 32P-labeled Alu, telomeric (TTAGGG)3 or HHV-6A (DR6) probes. After hybridization the membranes were washed & exposed to X-ray films. D & F) Densitometric analysis of relative binding of TRF2 to telomeric & viral DNA. Results of one experiment representative of three are presented & are expressed as signal after normalization to input. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32320442), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-56694_goat-polyclonal-trf-2-antibody-3102024155376.jpg)
![Immunocytochemistry/ Immunofluorescence: TRF-2 Antibody [NB100-56694] - TRF2 is required for IE2 localization with telomeres.U2OS cells were transduced with a lentiviral vector coding for a Dox inducible control shRNA (shCtrl) or a shRNA against TRF2 (shTRF2) & selected with puromycin +/- Dox for a week. A) Western blot analysis of TRF2 expression one week post selection. Membranes were also probed with anti-tubulin antibodies to show the input material loaded. B) One week post selection, +Dox cells were infected with HHV-6A for 48h & processed for IFA using anti-TRF2 (green) & anti-IE2 (red). Cells with IE2 in punctate form & cells with large patchy IE2, likely to represent VRC, are shown. Nuclei are outlined by dashed lines. C) The percentage of HHV-6A infected cells (from B) was estimated after counting a minimum of 700 cells & scoring the IE2+ ones. Results are expressed as mean %IE2+ cells ± SD. D) Mean percentage ± SD of IE2 localizing with telomeres in the presence (shCtrl +Dox) & absence (shTRF2 +Dox) of TRF2. Each dot represents the % of IE2 foci localizing with telomeres in one nucleus. ****p<0.0001. E) IF-FISH confocal images of shCtrl (+Dox) & shTRF2 (+Dox) cells analyzed for TRF2 (green), IE2 (red) & telomeres (cyan). Nuclei are outlined by dashed circles. Examples of IE2 localizing with telomeres (top row) or not found with telomeres (bottom row) are highlighted by the dashed polygons. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32320442), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-56694_goat-polyclonal-trf-2-antibody-31020241612657.jpg)
![Immunocytochemistry/ Immunofluorescence: TRF-2 Antibody [NB100-56694] - Binding of TRF2 to viral DNA during HHV-6A/B infection.A) Schematic representation of the HHV-6A/B genome. The DR6 probe used for hybridization is shown in red. Uninfected & HHV-6A-infected HSB-2 cells (B-D) or uninfected & HHV-6B-infectd Molt-3 cells (E-F) were analyzed for TRF2 binding to viral DNA using ChIP. The input was hybridized with Alu probe to assess quantity of starting material. Anti-IgG (negative control), anti-PolII (positive control) or TRF2 antibodies were used for immunoprecipitation. B) QPCR detection of GAPDH DNA following ChIP. Results are expressed as fold increase over control IgG. C & E) Eluted DNA was hybridized with 32P-labeled Alu, telomeric (TTAGGG)3 or HHV-6A (DR6) probes. After hybridization the membranes were washed & exposed to X-ray films. D & F) Densitometric analysis of relative binding of TRF2 to telomeric & viral DNA. Results of one experiment representative of three are presented & are expressed as signal after normalization to input. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32320442), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-56694_goat-polyclonal-trf-2-antibody-310202415523926.jpg)
![Immunocytochemistry/ Immunofluorescence: TRF-2 Antibody [NB100-56694] - A) A stick diagram of the IE2 protein with various domains identified is presented. B) Colocalization of HHV-6A IE2 protein with telomeres in the absence of viral DNA. U2OS cells were transfected with an empty vector, with IE2 expression vector or with IE2 delta 1290–1500 expression vector. Forty-eight hours later cells were processed for dual color immunofluorescence. Telomeres were labeled in cyan & IE2 in red. Nuclei are outlined by dashed lines. Examples of IE2 colocalizing with telomeres are presented in a 3D view (white arrows). C) The graph represents the mean ± SD % of WT IE2 & delta 1290–1500 IE2 localizing with telomeres. D) Lack of colocalization between HHV-6A p41 & telomeres in uninfected cells. U2OS cells were transfected with an empty vector or with a p41 expression vector. Forty-eight hours later cells were processed for dual color immunofluorescence. TRF2 was labeled green, p41 in red & nuclei outlined by a dashed line. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32320442), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-56694_goat-polyclonal-trf-2-antibody-310202415541930.jpg)
![Immunocytochemistry/ Immunofluorescence: TRF-2 Antibody [NB100-56694] - Colocalization of shelterin complex proteins & HHV-6A IE2 protein at VRC & cellular telomeres.A) U2OS cells were mock-infected or infected with HHV-6A for 48h after which cells were processed for IF-FISH. Telomeres were labeled in magenta, TRF2 in green & IE2 in red. The panels in the middle row show images of cells with IE2 patches overlapping with large, diffuse TRF2 & telomeric staining (rectangles). The panels in the third row represent infected cells with punctate IE2 pattern colocalizing with TRF2 & telomeres (dashed squares). The colocalization of IE2, TRF2 & telomeres are shown in both 2D & 3D images. B) Uninfected & HHV-6A-infected U2OS cells were transfected with an empty vector, a myc-tagged-TRF1 expression vector. Forty-eight hours later cells were processed for IF-FISH. TRF1 was labeled in green & IE2 in red. Nuclei were stained with DAPI. Images on the far right show 2D colocalization of TRF1 with IE2. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32320442), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-56694_goat-polyclonal-trf-2-antibody-31020241612621.jpg)